---
_id: '9363'
abstract:
- lang: eng
text: Optogenetics has been harnessed to shed new mechanistic light on current and
future therapeutic strategies. This has been to date achieved by the regulation
of ion flow and electrical signals in neuronal cells and neural circuits that
are known to be affected by disease. In contrast, the optogenetic delivery of
trophic biochemical signals, which support cell survival and are implicated in
degenerative disorders, has never been demonstrated in an animal model of disease.
Here, we reengineered the human and Drosophila melanogaster REarranged during
Transfection (hRET and dRET) receptors to be activated by light, creating one-component
optogenetic tools termed Opto-hRET and Opto-dRET. Upon blue light stimulation,
these receptors robustly induced the MAPK/ERK proliferative signaling pathway
in cultured cells. In PINK1B9 flies that exhibit loss of PTEN-induced putative
kinase 1 (PINK1), a kinase associated with familial Parkinson’s disease (PD),
light activation of Opto-dRET suppressed mitochondrial defects, tissue degeneration
and behavioral deficits. In human cells with PINK1 loss-of-function, mitochondrial
fragmentation was rescued using Opto-dRET via the PI3K/NF-кB pathway. Our results
demonstrate that a light-activated receptor can ameliorate disease hallmarks in
a genetic model of PD. The optogenetic delivery of trophic signals is cell type-specific
and reversible and thus has the potential to inspire novel strategies towards
a spatio-temporal regulation of tissue repair.
acknowledgement: We thank R. Cagan, A. Whitworth and J. Nagpal for fly lines and advice,
S. Herlitze for provision of a tissue culture illuminator, and Verian Bader for
help with statistical analysis.
article_processing_charge: No
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Nikolas
full_name: Furthmann, Nikolas
last_name: Furthmann
- first_name: Samuel H.
full_name: Crossman, Samuel H.
last_name: Crossman
- first_name: Alexandra Madelaine
full_name: Tichy, Alexandra Madelaine
last_name: Tichy
- first_name: Nina
full_name: Hoyer, Nina
last_name: Hoyer
- first_name: Meike
full_name: Petersen, Meike
last_name: Petersen
- first_name: Vanessa
full_name: Zheden, Vanessa
id: 39C5A68A-F248-11E8-B48F-1D18A9856A87
last_name: Zheden
- first_name: Julia
full_name: Bicher, Julia
id: 3CCBB46E-F248-11E8-B48F-1D18A9856A87
last_name: Bicher
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Attila
full_name: György, Attila
id: 3BCEDBE0-F248-11E8-B48F-1D18A9856A87
last_name: György
orcid: 0000-0002-1819-198X
- first_name: Daria E
full_name: Siekhaus, Daria E
id: 3D224B9E-F248-11E8-B48F-1D18A9856A87
last_name: Siekhaus
orcid: 0000-0001-8323-8353
- first_name: Peter
full_name: Soba, Peter
last_name: Soba
- first_name: Konstanze F.
full_name: Winklhofer, Konstanze F.
last_name: Winklhofer
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Inglés Prieto Á, Furthmann N, Crossman SH, et al. Optogenetic delivery of trophic
signals in a genetic model of Parkinson’s disease. PLoS genetics. 2021;17(4):e1009479.
doi:10.1371/journal.pgen.1009479
apa: Inglés Prieto, Á., Furthmann, N., Crossman, S. H., Tichy, A. M., Hoyer, N.,
Petersen, M., … Janovjak, H. L. (2021). Optogenetic delivery of trophic signals
in a genetic model of Parkinson’s disease. PLoS Genetics. Public Library
of Science. https://doi.org/10.1371/journal.pgen.1009479
chicago: Inglés Prieto, Álvaro, Nikolas Furthmann, Samuel H. Crossman, Alexandra
Madelaine Tichy, Nina Hoyer, Meike Petersen, Vanessa Zheden, et al. “Optogenetic
Delivery of Trophic Signals in a Genetic Model of Parkinson’s Disease.” PLoS
Genetics. Public Library of Science, 2021. https://doi.org/10.1371/journal.pgen.1009479.
ieee: Á. Inglés Prieto et al., “Optogenetic delivery of trophic signals in
a genetic model of Parkinson’s disease,” PLoS genetics, vol. 17, no. 4.
Public Library of Science, p. e1009479, 2021.
ista: Inglés Prieto Á, Furthmann N, Crossman SH, Tichy AM, Hoyer N, Petersen M,
Zheden V, Bicher J, Gschaider-Reichhart E, György A, Siekhaus DE, Soba P, Winklhofer
KF, Janovjak HL. 2021. Optogenetic delivery of trophic signals in a genetic model
of Parkinson’s disease. PLoS genetics. 17(4), e1009479.
mla: Inglés Prieto, Álvaro, et al. “Optogenetic Delivery of Trophic Signals in a
Genetic Model of Parkinson’s Disease.” PLoS Genetics, vol. 17, no. 4, Public
Library of Science, 2021, p. e1009479, doi:10.1371/journal.pgen.1009479.
short: Á. Inglés Prieto, N. Furthmann, S.H. Crossman, A.M. Tichy, N. Hoyer, M. Petersen,
V. Zheden, J. Bicher, E. Gschaider-Reichhart, A. György, D.E. Siekhaus, P. Soba,
K.F. Winklhofer, H.L. Janovjak, PLoS Genetics 17 (2021) e1009479.
date_created: 2021-05-02T22:01:29Z
date_published: 2021-04-01T00:00:00Z
date_updated: 2023-08-08T13:17:47Z
day: '01'
ddc:
- '570'
department:
- _id: EM-Fac
- _id: LoSw
- _id: DaSi
doi: 10.1371/journal.pgen.1009479
external_id:
isi:
- '000640606700001'
file:
- access_level: open_access
checksum: 82a74668f863e8dfb22fdd4f845c92ce
content_type: application/pdf
creator: kschuh
date_created: 2021-05-04T09:05:27Z
date_updated: 2021-05-04T09:05:27Z
file_id: '9369'
file_name: 2021_PLOS_Ingles-Prieto.pdf
file_size: 3072764
relation: main_file
success: 1
file_date_updated: 2021-05-04T09:05:27Z
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intvolume: ' 17'
isi: 1
issue: '4'
language:
- iso: eng
month: '04'
oa: 1
oa_version: Published Version
page: e1009479
publication: PLoS genetics
publication_identifier:
eissn:
- '15537404'
publication_status: published
publisher: Public Library of Science
quality_controlled: '1'
scopus_import: '1'
status: public
title: Optogenetic delivery of trophic signals in a genetic model of Parkinson's disease
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 17
year: '2021'
...
---
_id: '10144'
abstract:
- lang: eng
text: FGFs and their high-affinity receptors (FGFRs) play key roles in development,
tissue repair, and disease. Because FGFRs bind overlapping sets of ligands, their
individual functions cannot be determined using ligand stimulation. Here, we generated
a light-activated FGFR2 variant (OptoR2) to selectively activate signaling by
the major FGFR in keratinocytes. Illumination of OptoR2-expressing HEK 293T cells
activated FGFR signaling with remarkable temporal precision and promoted cell
migration and proliferation. In murine and human keratinocytes, OptoR2 activation
rapidly induced the classical FGFR signaling pathways and expression of FGF target
genes. Surprisingly, multi-level counter-regulation occurred in keratinocytes
in vitro and in transgenic mice in vivo, including OptoR2 down-regulation and
loss of responsiveness to light activation. These results demonstrate unexpected
cell type-specific limitations of optogenetic FGFRs in long-term in vitro and
in vivo settings and highlight the complex consequences of transferring optogenetic
cell signaling tools into their relevant cellular contexts.
acknowledgement: We thank Connor Richterich and Patricia Reinert, ETH Zurich, for
invaluable experimental help; Manuela Pérez Berlanga, University Zurich, for help
with the confocal imaging; Lukas Fischer for help with electrical engineering; Thomas
Hennek, Sol Taguinod, and Dr. Stephan Sonntag, EPIC Phenomics Center, ETH Zürich,
for the generation and maintenance of K14-OptoR2 mice; and Dr. Petra Boukamp, Leibniz
Institute, Düsseldorf, Germany, for early-passage HaCaT keratinocytes. This work
was supported by the ETH Zurich (grant ETH-06 15-1 to S Werner and L Maddaluno),
the Swiss National Science Foundation (grant 31003B-189364 to S Werner), and a Marie
Curie postdoctoral fellowship from the European Union (to L Maddaluno).
article_number: e202101100
article_processing_charge: Yes
article_type: original
author:
- first_name: Theresa
full_name: Rauschendorfer, Theresa
last_name: Rauschendorfer
- first_name: Selina
full_name: Gurri, Selina
last_name: Gurri
- first_name: Irina
full_name: Heggli, Irina
last_name: Heggli
- first_name: Luigi
full_name: Maddaluno, Luigi
last_name: Maddaluno
- first_name: Michael
full_name: Meyer, Michael
last_name: Meyer
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Sabine
full_name: Werner, Sabine
last_name: Werner
citation:
ama: Rauschendorfer T, Gurri S, Heggli I, et al. Acute and chronic effects of a
light-activated FGF receptor in keratinocytes in vitro and in mice. Life Science
Alliance. 2021;4(11). doi:10.26508/lsa.202101100
apa: Rauschendorfer, T., Gurri, S., Heggli, I., Maddaluno, L., Meyer, M., Inglés
Prieto, Á., … Werner, S. (2021). Acute and chronic effects of a light-activated
FGF receptor in keratinocytes in vitro and in mice. Life Science Alliance.
Life Science Alliance. https://doi.org/10.26508/lsa.202101100
chicago: Rauschendorfer, Theresa, Selina Gurri, Irina Heggli, Luigi Maddaluno, Michael
Meyer, Álvaro Inglés Prieto, Harald L Janovjak, and Sabine Werner. “Acute and
Chronic Effects of a Light-Activated FGF Receptor in Keratinocytes in Vitro and
in Mice.” Life Science Alliance. Life Science Alliance, 2021. https://doi.org/10.26508/lsa.202101100.
ieee: T. Rauschendorfer et al., “Acute and chronic effects of a light-activated
FGF receptor in keratinocytes in vitro and in mice,” Life Science Alliance,
vol. 4, no. 11. Life Science Alliance, 2021.
ista: Rauschendorfer T, Gurri S, Heggli I, Maddaluno L, Meyer M, Inglés Prieto Á,
Janovjak HL, Werner S. 2021. Acute and chronic effects of a light-activated FGF
receptor in keratinocytes in vitro and in mice. Life Science Alliance. 4(11),
e202101100.
mla: Rauschendorfer, Theresa, et al. “Acute and Chronic Effects of a Light-Activated
FGF Receptor in Keratinocytes in Vitro and in Mice.” Life Science Alliance,
vol. 4, no. 11, e202101100, Life Science Alliance, 2021, doi:10.26508/lsa.202101100.
short: T. Rauschendorfer, S. Gurri, I. Heggli, L. Maddaluno, M. Meyer, Á. Inglés
Prieto, H.L. Janovjak, S. Werner, Life Science Alliance 4 (2021).
date_created: 2021-10-17T22:01:16Z
date_published: 2021-09-21T00:00:00Z
date_updated: 2022-08-31T14:01:56Z
day: '21'
ddc:
- '576'
doi: 10.26508/lsa.202101100
extern: '1'
external_id:
pmid:
- '34548382'
file:
- access_level: open_access
checksum: 89fb95b211dbe8678809e7cca4626952
content_type: application/pdf
creator: cchlebak
date_created: 2021-10-18T14:48:06Z
date_updated: 2021-10-18T14:48:06Z
file_id: '10152'
file_name: 2021_LifeScAlliance_Rauschendorfer.pdf
file_size: 2055981
relation: main_file
success: 1
file_date_updated: 2021-10-18T14:48:06Z
has_accepted_license: '1'
intvolume: ' 4'
issue: '11'
language:
- iso: eng
month: '09'
oa: 1
oa_version: Published Version
pmid: 1
publication: Life Science Alliance
publication_identifier:
eissn:
- 2575-1077
publication_status: published
publisher: Life Science Alliance
quality_controlled: '1'
scopus_import: '1'
status: public
title: Acute and chronic effects of a light-activated FGF receptor in keratinocytes
in vitro and in mice
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 4
year: '2021'
...
---
_id: '1100'
abstract:
- lang: eng
text: During metazoan development, the temporal pattern of morphogen signaling is
critical for organizing cell fates in space and time. Yet, tools for temporally
controlling morphogen signaling within the embryo are still scarce. Here, we developed
a photoactivatable Nodal receptor to determine how the temporal pattern of Nodal
signaling affects cell fate specification during zebrafish gastrulation. By using
this receptor to manipulate the duration of Nodal signaling in vivo by light,
we show that extended Nodal signaling within the organizer promotes prechordal
plate specification and suppresses endoderm differentiation. Endoderm differentiation
is suppressed by extended Nodal signaling inducing expression of the transcriptional
repressor goosecoid (gsc) in prechordal plate progenitors, which in turn restrains
Nodal signaling from upregulating the endoderm differentiation gene sox17 within
these cells. Thus, optogenetic manipulation of Nodal signaling identifies a critical
role of Nodal signaling duration for organizer cell fate specification during
gastrulation.
acknowledged_ssus:
- _id: SSU
acknowledgement: 'We are grateful to members of the C.-P.H. and H.J. labs for discussions,
R. Hauschild and the different Scientific Service Units at IST Austria for technical
help, M. Dravecka for performing initial experiments, A. Schier for reading an earlier
version of the manuscript, K.W. Rogers for technical help, and C. Hill, A. Bruce,
and L. Solnica-Krezel for sending plasmids. This work was supported by grants from
the Austrian Science Foundation (FWF): (T560-B17) and (I 812-B12) to V.R. and C.-P.H.,
and from the European Union (EU FP7): (6275) to H.J. A.I.-P. is supported by a Ramon
Areces fellowship.'
author:
- first_name: Keisuke
full_name: Sako, Keisuke
id: 3BED66BE-F248-11E8-B48F-1D18A9856A87
last_name: Sako
orcid: 0000-0002-6453-8075
- first_name: Saurabh
full_name: Pradhan, Saurabh
last_name: Pradhan
- first_name: Vanessa
full_name: Barone, Vanessa
id: 419EECCC-F248-11E8-B48F-1D18A9856A87
last_name: Barone
orcid: 0000-0003-2676-3367
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Patrick
full_name: Mueller, Patrick
last_name: Mueller
- first_name: Verena
full_name: Ruprecht, Verena
id: 4D71A03A-F248-11E8-B48F-1D18A9856A87
last_name: Ruprecht
orcid: 0000-0003-4088-8633
- first_name: Daniel
full_name: Capek, Daniel
id: 31C42484-F248-11E8-B48F-1D18A9856A87
last_name: Capek
orcid: 0000-0001-5199-9940
- first_name: Sanjeev
full_name: Galande, Sanjeev
last_name: Galande
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Carl-Philipp J
full_name: Heisenberg, Carl-Philipp J
id: 39427864-F248-11E8-B48F-1D18A9856A87
last_name: Heisenberg
orcid: 0000-0002-0912-4566
citation:
ama: Sako K, Pradhan S, Barone V, et al. Optogenetic control of nodal signaling
reveals a temporal pattern of nodal signaling regulating cell fate specification
during gastrulation. Cell Reports. 2016;16(3):866-877. doi:10.1016/j.celrep.2016.06.036
apa: Sako, K., Pradhan, S., Barone, V., Inglés Prieto, Á., Mueller, P., Ruprecht,
V., … Heisenberg, C.-P. J. (2016). Optogenetic control of nodal signaling reveals
a temporal pattern of nodal signaling regulating cell fate specification during
gastrulation. Cell Reports. Cell Press. https://doi.org/10.1016/j.celrep.2016.06.036
chicago: Sako, Keisuke, Saurabh Pradhan, Vanessa Barone, Álvaro Inglés Prieto, Patrick
Mueller, Verena Ruprecht, Daniel Capek, Sanjeev Galande, Harald L Janovjak, and
Carl-Philipp J Heisenberg. “Optogenetic Control of Nodal Signaling Reveals a Temporal
Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.”
Cell Reports. Cell Press, 2016. https://doi.org/10.1016/j.celrep.2016.06.036.
ieee: K. Sako et al., “Optogenetic control of nodal signaling reveals a temporal
pattern of nodal signaling regulating cell fate specification during gastrulation,”
Cell Reports, vol. 16, no. 3. Cell Press, pp. 866–877, 2016.
ista: Sako K, Pradhan S, Barone V, Inglés Prieto Á, Mueller P, Ruprecht V, Capek
D, Galande S, Janovjak HL, Heisenberg C-PJ. 2016. Optogenetic control of nodal
signaling reveals a temporal pattern of nodal signaling regulating cell fate specification
during gastrulation. Cell Reports. 16(3), 866–877.
mla: Sako, Keisuke, et al. “Optogenetic Control of Nodal Signaling Reveals a Temporal
Pattern of Nodal Signaling Regulating Cell Fate Specification during Gastrulation.”
Cell Reports, vol. 16, no. 3, Cell Press, 2016, pp. 866–77, doi:10.1016/j.celrep.2016.06.036.
short: K. Sako, S. Pradhan, V. Barone, Á. Inglés Prieto, P. Mueller, V. Ruprecht,
D. Capek, S. Galande, H.L. Janovjak, C.-P.J. Heisenberg, Cell Reports 16 (2016)
866–877.
date_created: 2018-12-11T11:50:08Z
date_published: 2016-07-19T00:00:00Z
date_updated: 2024-03-25T23:30:13Z
day: '19'
ddc:
- '570'
- '576'
department:
- _id: CaHe
- _id: HaJa
doi: 10.1016/j.celrep.2016.06.036
ec_funded: 1
file:
- access_level: open_access
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:11:04Z
date_updated: 2018-12-12T10:11:04Z
file_id: '4857'
file_name: IST-2017-754-v1+1_1-s2.0-S2211124716307768-main.pdf
file_size: 3921947
relation: main_file
file_date_updated: 2018-12-12T10:11:04Z
has_accepted_license: '1'
intvolume: ' 16'
issue: '3'
language:
- iso: eng
month: '07'
oa: 1
oa_version: Published Version
page: 866 - 877
project:
- _id: 2529486C-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: T 560-B17
name: Cell- and Tissue Mechanics in Zebrafish Germ Layer Formation
- _id: 2527D5CC-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: I 812-B12
name: Cell Cortex and Germ Layer Formation in Zebrafish Gastrulation
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
publication: Cell Reports
publication_status: published
publisher: Cell Press
publist_id: '6275'
pubrep_id: '754'
quality_controlled: '1'
related_material:
record:
- id: '961'
relation: dissertation_contains
status: public
- id: '50'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: Optogenetic control of nodal signaling reveals a temporal pattern of nodal
signaling regulating cell fate specification during gastrulation
tmp:
image: /images/cc_by.png
legal_code_url: https://creativecommons.org/licenses/by/4.0/legalcode
name: Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)
short: CC BY (4.0)
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 16
year: '2016'
...
---
_id: '1441'
abstract:
- lang: eng
text: 'Optogenetics and photopharmacology enable the spatio-temporal control of
cell and animal behavior by light. Although red light offers deep-tissue penetration
and minimal phototoxicity, very few red-light-sensitive optogenetic methods are
currently available. We have now developed a red-light-induced homodimerization
domain. We first showed that an optimized sensory domain of the cyanobacterial
phytochrome 1 can be expressed robustly and without cytotoxicity in human cells.
We then applied this domain to induce the dimerization of two receptor tyrosine
kinases—the fibroblast growth factor receptor 1 and the neurotrophin receptor
trkB. This new optogenetic method was then used to activate the MAPK/ERK pathway
non-invasively in mammalian tissue and in multicolor cell-signaling experiments.
The light-controlled dimerizer and red-light-activated receptor tyrosine kinases
will prove useful to regulate a variety of cellular processes with light. Go deep
with red: The sensory domain (S) of the cyanobacterial phytochrome 1 (CPH1) was
repurposed to induce the homodimerization of proteins in living cells by red light.
By using this domain, light-activated protein kinases were engineered that can
be activated orthogonally from many fluorescent proteins and through mammalian
tissue. Pr/Pfr=red-/far-red-absorbing state of CPH1.'
acknowledgement: 'A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by
the graduate program MolecularDrugTargets (Austrian Science Fund (FWF): W1232) and
a FemTech fellowship (Austrian Research Promotion Agency: 3580812).'
author:
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Alexandra-Madelaine
full_name: Tichy, Alexandra-Madelaine
id: 29D8BB2C-F248-11E8-B48F-1D18A9856A87
last_name: Tichy
- first_name: Catherine
full_name: Mckenzie, Catherine
id: 3EEDE19A-F248-11E8-B48F-1D18A9856A87
last_name: Mckenzie
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Gschaider-Reichhart E, Inglés Prieto Á, Tichy A-M, Mckenzie C, Janovjak HL.
A phytochrome sensory domain permits receptor activation by red light. Angewandte
Chemie - International Edition. 2016;55(21):6339-6342. doi:10.1002/anie.201601736
apa: Gschaider-Reichhart, E., Inglés Prieto, Á., Tichy, A.-M., Mckenzie, C., &
Janovjak, H. L. (2016). A phytochrome sensory domain permits receptor activation
by red light. Angewandte Chemie - International Edition. Wiley. https://doi.org/10.1002/anie.201601736
chicago: Gschaider-Reichhart, Eva, Álvaro Inglés Prieto, Alexandra-Madelaine Tichy,
Catherine Mckenzie, and Harald L Janovjak. “A Phytochrome Sensory Domain Permits
Receptor Activation by Red Light.” Angewandte Chemie - International Edition.
Wiley, 2016. https://doi.org/10.1002/anie.201601736.
ieee: E. Gschaider-Reichhart, Á. Inglés Prieto, A.-M. Tichy, C. Mckenzie, and H.
L. Janovjak, “A phytochrome sensory domain permits receptor activation by red
light,” Angewandte Chemie - International Edition, vol. 55, no. 21. Wiley,
pp. 6339–6342, 2016.
ista: Gschaider-Reichhart E, Inglés Prieto Á, Tichy A-M, Mckenzie C, Janovjak HL.
2016. A phytochrome sensory domain permits receptor activation by red light. Angewandte
Chemie - International Edition. 55(21), 6339–6342.
mla: Gschaider-Reichhart, Eva, et al. “A Phytochrome Sensory Domain Permits Receptor
Activation by Red Light.” Angewandte Chemie - International Edition, vol.
55, no. 21, Wiley, 2016, pp. 6339–42, doi:10.1002/anie.201601736.
short: E. Gschaider-Reichhart, Á. Inglés Prieto, A.-M. Tichy, C. Mckenzie, H.L.
Janovjak, Angewandte Chemie - International Edition 55 (2016) 6339–6342.
date_created: 2018-12-11T11:52:02Z
date_published: 2016-05-17T00:00:00Z
date_updated: 2023-09-07T12:49:08Z
day: '17'
ddc:
- '571'
- '576'
department:
- _id: HaJa
doi: 10.1002/anie.201601736
ec_funded: 1
file:
- access_level: open_access
checksum: 26da07960e57ac4750b54179197ce57f
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:17:03Z
date_updated: 2020-07-14T12:44:55Z
file_id: '5255'
file_name: IST-2017-840-v1+1_reichhart.pdf
file_size: 1268662
relation: main_file
file_date_updated: 2020-07-14T12:44:55Z
has_accepted_license: '1'
intvolume: ' 55'
issue: '21'
language:
- iso: eng
month: '05'
oa: 1
oa_version: Submitted Version
page: 6339 - 6342
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255A6082-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1232-B24
name: Molecular Drug Targets
publication: Angewandte Chemie - International Edition
publication_status: published
publisher: Wiley
publist_id: '5755'
pubrep_id: '840'
quality_controlled: '1'
related_material:
record:
- id: '418'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: A phytochrome sensory domain permits receptor activation by red light
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 55
year: '2016'
...
---
_id: '1678'
abstract:
- lang: eng
text: High-throughput live-cell screens are intricate elements of systems biology
studies and drug discovery pipelines. Here, we demonstrate an optogenetics-assisted
method that avoids the need for chemical activators and reporters, reduces the
number of operational steps and increases information content in a cell-based
small-molecule screen against human protein kinases, including an orphan receptor
tyrosine kinase. This blueprint for all-optical screening can be adapted to many
drug targets and cellular processes.
acknowledgement: 'This work was supported by grants from the European Union Seventh
Framework Programme (CIG-303564 to H.J. and ERC-StG-311166 to S.M.B.N.), the Human
Frontier Science Program (RGY0084_2012 to H.J.) and the Herzfelder Foundation (to
M.G.). A.I.-P. was supported by a Ramon Areces fellowship, and E.R. by the graduate
program MolecularDrugTargets (Austrian Science Fund (FWF): W 1232) and a FemTech
fellowship (3580812 Austrian Research Promotion Agency).'
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Markus
full_name: Muellner, Markus
last_name: Muellner
- first_name: Matthias
full_name: Nowak, Matthias
id: 30845DAA-F248-11E8-B48F-1D18A9856A87
last_name: Nowak
- first_name: Sebastian
full_name: Nijman, Sebastian
last_name: Nijman
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, et al. Light-assisted small-molecule
screening against protein kinases. Nature Chemical Biology. 2015;11(12):952-954.
doi:10.1038/nchembio.1933
apa: Inglés Prieto, Á., Gschaider-Reichhart, E., Muellner, M., Nowak, M., Nijman,
S., Grusch, M., & Janovjak, H. L. (2015). Light-assisted small-molecule screening
against protein kinases. Nature Chemical Biology. Nature Publishing Group.
https://doi.org/10.1038/nchembio.1933
chicago: Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Markus Muellner, Matthias
Nowak, Sebastian Nijman, Michael Grusch, and Harald L Janovjak. “Light-Assisted
Small-Molecule Screening against Protein Kinases.” Nature Chemical Biology.
Nature Publishing Group, 2015. https://doi.org/10.1038/nchembio.1933.
ieee: Á. Inglés Prieto et al., “Light-assisted small-molecule screening against
protein kinases,” Nature Chemical Biology, vol. 11, no. 12. Nature Publishing
Group, pp. 952–954, 2015.
ista: Inglés Prieto Á, Gschaider-Reichhart E, Muellner M, Nowak M, Nijman S, Grusch
M, Janovjak HL. 2015. Light-assisted small-molecule screening against protein
kinases. Nature Chemical Biology. 11(12), 952–954.
mla: Inglés Prieto, Álvaro, et al. “Light-Assisted Small-Molecule Screening against
Protein Kinases.” Nature Chemical Biology, vol. 11, no. 12, Nature Publishing
Group, 2015, pp. 952–54, doi:10.1038/nchembio.1933.
short: Á. Inglés Prieto, E. Gschaider-Reichhart, M. Muellner, M. Nowak, S. Nijman,
M. Grusch, H.L. Janovjak, Nature Chemical Biology 11 (2015) 952–954.
date_created: 2018-12-11T11:53:25Z
date_published: 2015-10-12T00:00:00Z
date_updated: 2023-09-07T12:49:09Z
day: '12'
ddc:
- '571'
department:
- _id: HaJa
- _id: LifeSc
doi: 10.1038/nchembio.1933
ec_funded: 1
file:
- access_level: open_access
checksum: e9fb251dfcb7cd209b83f17867e61321
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:10:51Z
date_updated: 2020-07-14T12:45:12Z
file_id: '4842'
file_name: IST-2017-837-v1+1_ingles-prieto.pdf
file_size: 1308364
relation: main_file
file_date_updated: 2020-07-14T12:45:12Z
has_accepted_license: '1'
intvolume: ' 11'
issue: '12'
language:
- iso: eng
month: '10'
oa: 1
oa_version: Submitted Version
page: 952 - 954
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
- _id: 255A6082-B435-11E9-9278-68D0E5697425
call_identifier: FWF
grant_number: W1232-B24
name: Molecular Drug Targets
publication: Nature Chemical Biology
publication_status: published
publisher: Nature Publishing Group
publist_id: '5471'
pubrep_id: '837'
quality_controlled: '1'
related_material:
record:
- id: '418'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: Light-assisted small-molecule screening against protein kinases
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 11
year: '2015'
...
---
_id: '1867'
abstract:
- lang: eng
text: Cultured mammalian cells essential are model systems in basic biology research,
production platforms of proteins for medical use, and testbeds in synthetic biology.
Flavin cofactors, in particular flavin mononucleotide (FMN) and flavin adenine
dinucleotide (FAD), are critical for cellular redox reactions and sense light
in naturally occurring photoreceptors and optogenetic tools. Here, we quantified
flavin contents of commonly used mammalian cell lines. We first compared three
procedures for extraction of free and noncovalently protein-bound flavins and
verified extraction using fluorescence spectroscopy. For separation, two CE methods
with different BGEs were established, and detection was performed by LED-induced
fluorescence with limit of detections (LODs 0.5-3.8 nM). We found that riboflavin
(RF), FMN, and FAD contents varied significantly between cell lines. RF (3.1-14
amol/cell) and FAD (2.2-17.0 amol/cell) were the predominant flavins, while FMN
(0.46-3.4 amol/cell) was found at markedly lower levels. Observed flavin contents
agree with those previously extracted from mammalian tissues, yet reduced forms
of RF were detected that were not described previously. Quantification of flavins
in mammalian cell lines will allow a better understanding of cellular redox reactions
and optogenetic tools.
author:
- first_name: Jens
full_name: Hühner, Jens
last_name: Hühner
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Christian
full_name: Neusüß, Christian
last_name: Neusüß
- first_name: Michael
full_name: Lämmerhofer, Michael
last_name: Lämmerhofer
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis.
2015;36(4):518-525. doi:10.1002/elps.201400451
apa: Hühner, J., Inglés Prieto, Á., Neusüß, C., Lämmerhofer, M., & Janovjak,
H. L. (2015). Quantification of riboflavin, flavin mononucleotide, and flavin
adenine dinucleotide in mammalian model cells by CE with LED-induced fluorescence
detection. Electrophoresis. Wiley. https://doi.org/10.1002/elps.201400451
chicago: Hühner, Jens, Álvaro Inglés Prieto, Christian Neusüß, Michael Lämmerhofer,
and Harald L Janovjak. “Quantification of Riboflavin, Flavin Mononucleotide, and
Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced Fluorescence
Detection.” Electrophoresis. Wiley, 2015. https://doi.org/10.1002/elps.201400451.
ieee: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, and H. L. Janovjak,
“Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection,” Electrophoresis,
vol. 36, no. 4. Wiley, pp. 518–525, 2015.
ista: Hühner J, Inglés Prieto Á, Neusüß C, Lämmerhofer M, Janovjak HL. 2015. Quantification
of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide in mammalian
model cells by CE with LED-induced fluorescence detection. Electrophoresis. 36(4),
518–525.
mla: Hühner, Jens, et al. “Quantification of Riboflavin, Flavin Mononucleotide,
and Flavin Adenine Dinucleotide in Mammalian Model Cells by CE with LED-Induced
Fluorescence Detection.” Electrophoresis, vol. 36, no. 4, Wiley, 2015,
pp. 518–25, doi:10.1002/elps.201400451.
short: J. Hühner, Á. Inglés Prieto, C. Neusüß, M. Lämmerhofer, H.L. Janovjak, Electrophoresis
36 (2015) 518–525.
date_created: 2018-12-11T11:54:26Z
date_published: 2015-02-01T00:00:00Z
date_updated: 2021-01-12T06:53:43Z
day: '01'
department:
- _id: HaJa
doi: 10.1002/elps.201400451
ec_funded: 1
intvolume: ' 36'
issue: '4'
language:
- iso: eng
month: '02'
oa_version: None
page: 518 - 525
project:
- _id: 25548C20-B435-11E9-9278-68D0E5697425
call_identifier: FP7
grant_number: '303564'
name: Microbial Ion Channels for Synthetic Neurobiology
- _id: 255BFFFA-B435-11E9-9278-68D0E5697425
grant_number: RGY0084/2012
name: In situ real-time imaging of neurotransmitter signaling using designer optical
sensors (HFSP Young Investigator)
publication: Electrophoresis
publication_status: published
publisher: Wiley
publist_id: '5230'
pubrep_id: '836'
quality_controlled: '1'
scopus_import: 1
status: public
title: Quantification of riboflavin, flavin mononucleotide, and flavin adenine dinucleotide
in mammalian model cells by CE with LED-induced fluorescence detection
type: journal_article
user_id: 2DF688A6-F248-11E8-B48F-1D18A9856A87
volume: 36
year: '2015'
...
---
_id: '1844'
abstract:
- lang: eng
text: 'Local protein interactions ("molecular context" effects) dictate
amino acid replacements and can be described in terms of site-specific, energetic
preferences for any different amino acid. It has been recently debated whether
these preferences remain approximately constant during evolution or whether, due
to coevolution of sites, they change strongly. Such research highlights an unresolved
and fundamental issue with far-reaching implications for phylogenetic analysis
and molecular evolution modeling. Here, we take advantage of the recent availability
of phenotypically supported laboratory resurrections of Precambrian thioredoxins
and β-lactamases to experimentally address the change of site-specific amino acid
preferences over long geological timescales. Extensive mutational analyses support
the notion that evolutionary adjustment to a new amino acid may occur, but to
a large extent this is insufficient to erase the primitive preference for amino
acid replacements. Generally, site-specific amino acid preferences appear to remain
conserved throughout evolutionary history despite local sequence divergence. We
show such preference conservation to be readily understandable in molecular terms
and we provide crystallographic evidence for an intriguing structural-switch mechanism:
Energetic preference for an ancestral amino acid in a modern protein can be linked
to reorganization upon mutation to the ancestral local structure around the mutated
site. Finally, we point out that site-specific preference conservation naturally
leads to one plausible evolutionary explanation for the existence of intragenic
global suppressor mutations.'
author:
- first_name: Valeria
full_name: Risso, Valeria
last_name: Risso
- first_name: Fadia
full_name: Manssour Triedo, Fadia
last_name: Manssour Triedo
- first_name: Asuncion
full_name: Delgado Delgado, Asuncion
last_name: Delgado Delgado
- first_name: Rocio
full_name: Arco, Rocio
last_name: Arco
- first_name: Alicia
full_name: Barroso Deljesús, Alicia
last_name: Barroso Deljesús
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Raquel
full_name: Godoy Ruiz, Raquel
last_name: Godoy Ruiz
- first_name: Josè
full_name: Gavira, Josè
last_name: Gavira
- first_name: Eric
full_name: Gaucher, Eric
last_name: Gaucher
- first_name: Beatriz
full_name: Ibarra Molero, Beatriz
last_name: Ibarra Molero
- first_name: Jose
full_name: Sánchez Ruiz, Jose
last_name: Sánchez Ruiz
citation:
ama: Risso V, Manssour Triedo F, Delgado Delgado A, et al. Mutational studies on
resurrected ancestral proteins reveal conservation of site-specific amino acid
preferences throughout evolutionary history. Molecular Biology and Evolution.
2014;32(2):440-455. doi:10.1093/molbev/msu312
apa: Risso, V., Manssour Triedo, F., Delgado Delgado, A., Arco, R., Barroso Deljesús,
A., Inglés Prieto, Á., … Sánchez Ruiz, J. (2014). Mutational studies on resurrected
ancestral proteins reveal conservation of site-specific amino acid preferences
throughout evolutionary history. Molecular Biology and Evolution. Oxford
University Press. https://doi.org/10.1093/molbev/msu312
chicago: Risso, Valeria, Fadia Manssour Triedo, Asuncion Delgado Delgado, Rocio
Arco, Alicia Barroso Deljesús, Álvaro Inglés Prieto, Raquel Godoy Ruiz, et al.
“Mutational Studies on Resurrected Ancestral Proteins Reveal Conservation of Site-Specific
Amino Acid Preferences throughout Evolutionary History.” Molecular Biology
and Evolution. Oxford University Press, 2014. https://doi.org/10.1093/molbev/msu312.
ieee: V. Risso et al., “Mutational studies on resurrected ancestral proteins
reveal conservation of site-specific amino acid preferences throughout evolutionary
history,” Molecular Biology and Evolution, vol. 32, no. 2. Oxford University
Press, pp. 440–455, 2014.
ista: Risso V, Manssour Triedo F, Delgado Delgado A, Arco R, Barroso Deljesús A,
Inglés Prieto Á, Godoy Ruiz R, Gavira J, Gaucher E, Ibarra Molero B, Sánchez Ruiz
J. 2014. Mutational studies on resurrected ancestral proteins reveal conservation
of site-specific amino acid preferences throughout evolutionary history. Molecular
Biology and Evolution. 32(2), 440–455.
mla: Risso, Valeria, et al. “Mutational Studies on Resurrected Ancestral Proteins
Reveal Conservation of Site-Specific Amino Acid Preferences throughout Evolutionary
History.” Molecular Biology and Evolution, vol. 32, no. 2, Oxford University
Press, 2014, pp. 440–55, doi:10.1093/molbev/msu312.
short: V. Risso, F. Manssour Triedo, A. Delgado Delgado, R. Arco, A. Barroso Deljesús,
Á. Inglés Prieto, R. Godoy Ruiz, J. Gavira, E. Gaucher, B. Ibarra Molero, J. Sánchez
Ruiz, Molecular Biology and Evolution 32 (2014) 440–455.
date_created: 2018-12-11T11:54:19Z
date_published: 2014-11-12T00:00:00Z
date_updated: 2021-01-12T06:53:34Z
day: '12'
ddc:
- '571'
department:
- _id: HaJa
doi: 10.1093/molbev/msu312
file:
- access_level: open_access
checksum: 06215318e66be8f3e0c33abb07e9d3da
content_type: application/pdf
creator: system
date_created: 2018-12-12T10:16:56Z
date_updated: 2020-07-14T12:45:19Z
file_id: '5247'
file_name: IST-2016-430-v1+1_Mol_Biol_Evol-2015-Risso-440-55.pdf
file_size: 1545246
relation: main_file
file_date_updated: 2020-07-14T12:45:19Z
has_accepted_license: '1'
intvolume: ' 32'
issue: '2'
language:
- iso: eng
license: https://creativecommons.org/licenses/by-nc/4.0/
month: '11'
oa: 1
oa_version: Published Version
page: 440 - 455
publication: Molecular Biology and Evolution
publication_status: published
publisher: Oxford University Press
publist_id: '5257'
pubrep_id: '430'
quality_controlled: '1'
scopus_import: 1
status: public
title: Mutational studies on resurrected ancestral proteins reveal conservation of
site-specific amino acid preferences throughout evolutionary history
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 32
year: '2014'
...
---
_id: '2032'
abstract:
- lang: eng
text: As light-based control of fundamental signaling pathways is becoming a reality,
the field of optogenetics is rapidly moving beyond neuroscience. We have recently
developed receptor tyrosine kinases that are activated by light and control cell
proliferation, epithelial–mesenchymal transition, and angiogenic sprouting—cell
behaviors central to cancer progression.
article_number: e964045
author:
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Karin
full_name: Schelch, Karin
last_name: Schelch
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
citation:
ama: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
The optogenetic promise for oncology: Episode I. Molecular and Cellular Oncology.
2014;1(4). doi:10.4161/23723548.2014.964045'
apa: 'Inglés Prieto, Á., Gschaider-Reichhart, E., Schelch, K., Janovjak, H. L.,
& Grusch, M. (2014). The optogenetic promise for oncology: Episode I. Molecular
and Cellular Oncology. Taylor & Francis. https://doi.org/10.4161/23723548.2014.964045'
chicago: 'Inglés Prieto, Álvaro, Eva Gschaider-Reichhart, Karin Schelch, Harald
L Janovjak, and Michael Grusch. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology. Taylor & Francis, 2014. https://doi.org/10.4161/23723548.2014.964045.'
ieee: 'Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H. L. Janovjak, and
M. Grusch, “The optogenetic promise for oncology: Episode I,” Molecular and
Cellular Oncology, vol. 1, no. 4. Taylor & Francis, 2014.'
ista: 'Inglés Prieto Á, Gschaider-Reichhart E, Schelch K, Janovjak HL, Grusch M.
2014. The optogenetic promise for oncology: Episode I. Molecular and Cellular
Oncology. 1(4), e964045.'
mla: 'Inglés Prieto, Álvaro, et al. “The Optogenetic Promise for Oncology: Episode
I.” Molecular and Cellular Oncology, vol. 1, no. 4, e964045, Taylor &
Francis, 2014, doi:10.4161/23723548.2014.964045.'
short: Á. Inglés Prieto, E. Gschaider-Reichhart, K. Schelch, H.L. Janovjak, M. Grusch,
Molecular and Cellular Oncology 1 (2014).
date_created: 2018-12-11T11:55:19Z
date_published: 2014-12-31T00:00:00Z
date_updated: 2021-01-12T06:54:51Z
day: '31'
ddc:
- '570'
department:
- _id: HaJa
doi: 10.4161/23723548.2014.964045
file:
- access_level: open_access
checksum: 44e17ad40577ab46eb602e88a8b0b8fd
content_type: application/pdf
creator: kschuh
date_created: 2019-05-16T13:39:11Z
date_updated: 2020-07-14T12:45:26Z
file_id: '6464'
file_name: 2014_Taylor_Alvaro.pdf
file_size: 1765933
relation: main_file
file_date_updated: 2020-07-14T12:45:26Z
has_accepted_license: '1'
intvolume: ' 1'
issue: '4'
language:
- iso: eng
month: '12'
oa: 1
oa_version: Published Version
publication: Molecular and Cellular Oncology
publication_status: published
publisher: Taylor & Francis
publist_id: '5040'
quality_controlled: '1'
scopus_import: 1
status: public
title: 'The optogenetic promise for oncology: Episode I'
tmp:
image: /images/cc_by_nc.png
legal_code_url: https://creativecommons.org/licenses/by-nc/4.0/legalcode
name: Creative Commons Attribution-NonCommercial 4.0 International (CC BY-NC 4.0)
short: CC BY-NC (4.0)
type: journal_article
user_id: 3E5EF7F0-F248-11E8-B48F-1D18A9856A87
volume: 1
year: '2014'
...
---
_id: '2084'
abstract:
- lang: eng
text: Receptor tyrosine kinases (RTKs) are a large family of cell surface receptors
that sense growth factors and hormones and regulate a variety of cell behaviours
in health and disease. Contactless activation of RTKs with spatial and temporal
precision is currently not feasible. Here, we generated RTKs that are insensitive
to endogenous ligands but can be selectively activated by low-intensity blue light.
We screened light-oxygen-voltage (LOV)-sensing domains for their ability to activate
RTKs by light-activated dimerization. Incorporation of LOV domains found in aureochrome
photoreceptors of stramenopiles resulted in robust activation of the fibroblast
growth factor receptor 1 (FGFR1), epidermal growth factor receptor (EGFR) and
rearranged during transfection (RET). In human cancer and endothelial cells, light
induced cellular signalling with spatial and temporal precision. Furthermore,
light faithfully mimicked complex mitogenic and morphogenic cell behaviour induced
by growth factors. RTKs under optical control (Opto-RTKs) provide a powerful optogenetic
approach to actuate cellular signals and manipulate cell behaviour.
acknowledgement: European Union Seventh Framework Programme; Human Frontier Science
Program; Oesterreichische Nationalbank Anniversary Fund 14211; Austrian Research
Promotion Agency; FemTech
author:
- first_name: Michael
full_name: Grusch, Michael
last_name: Grusch
- first_name: Karin
full_name: Schelch, Karin
last_name: Schelch
- first_name: Robert
full_name: Riedler, Robert
last_name: Riedler
- first_name: Eva
full_name: Gschaider-Reichhart, Eva
id: 3FEE232A-F248-11E8-B48F-1D18A9856A87
last_name: Gschaider-Reichhart
orcid: 0000-0002-7218-7738
- first_name: Christopher
full_name: Differ, Christopher
last_name: Differ
- first_name: Walter
full_name: Berger, Walter
last_name: Berger
- first_name: Álvaro
full_name: Inglés Prieto, Álvaro
id: 2A9DB292-F248-11E8-B48F-1D18A9856A87
last_name: Inglés Prieto
orcid: 0000-0002-5409-8571
- first_name: Harald L
full_name: Janovjak, Harald L
id: 33BA6C30-F248-11E8-B48F-1D18A9856A87
last_name: Janovjak
orcid: 0000-0002-8023-9315
citation:
ama: Grusch M, Schelch K, Riedler R, et al. Spatio-temporally precise activation
of engineered receptor tyrosine kinases by light. EMBO Journal. 2014;33(15):1713-1726.
doi:10.15252/embj.201387695
apa: Grusch, M., Schelch, K., Riedler, R., Gschaider-Reichhart, E., Differ, C.,
Berger, W., … Janovjak, H. L. (2014). Spatio-temporally precise activation of
engineered receptor tyrosine kinases by light. EMBO Journal. Wiley-Blackwell.
https://doi.org/10.15252/embj.201387695
chicago: Grusch, Michael, Karin Schelch, Robert Riedler, Eva Gschaider-Reichhart,
Christopher Differ, Walter Berger, Álvaro Inglés Prieto, and Harald L Janovjak.
“Spatio-Temporally Precise Activation of Engineered Receptor Tyrosine Kinases
by Light.” EMBO Journal. Wiley-Blackwell, 2014. https://doi.org/10.15252/embj.201387695.
ieee: M. Grusch et al., “Spatio-temporally precise activation of engineered
receptor tyrosine kinases by light,” EMBO Journal, vol. 33, no. 15. Wiley-Blackwell,
pp. 1713–1726, 2014.
ista: Grusch M, Schelch K, Riedler R, Gschaider-Reichhart E, Differ C, Berger W,
Inglés Prieto Á, Janovjak HL. 2014. Spatio-temporally precise activation of engineered
receptor tyrosine kinases by light. EMBO Journal. 33(15), 1713–1726.
mla: Grusch, Michael, et al. “Spatio-Temporally Precise Activation of Engineered
Receptor Tyrosine Kinases by Light.” EMBO Journal, vol. 33, no. 15, Wiley-Blackwell,
2014, pp. 1713–26, doi:10.15252/embj.201387695.
short: M. Grusch, K. Schelch, R. Riedler, E. Gschaider-Reichhart, C. Differ, W.
Berger, Á. Inglés Prieto, H.L. Janovjak, EMBO Journal 33 (2014) 1713–1726.
date_created: 2018-12-11T11:55:37Z
date_published: 2014-07-01T00:00:00Z
date_updated: 2023-09-07T12:49:09Z
day: '01'
department:
- _id: HaJa
doi: 10.15252/embj.201387695
intvolume: ' 33'
issue: '15'
language:
- iso: eng
main_file_link:
- open_access: '1'
url: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4194103/
month: '07'
oa: 1
oa_version: Submitted Version
page: 1713 - 1726
publication: EMBO Journal
publication_status: published
publisher: Wiley-Blackwell
publist_id: '4953'
quality_controlled: '1'
related_material:
record:
- id: '418'
relation: dissertation_contains
status: public
scopus_import: 1
status: public
title: Spatio-temporally precise activation of engineered receptor tyrosine kinases
by light
type: journal_article
user_id: 4435EBFC-F248-11E8-B48F-1D18A9856A87
volume: 33
year: '2014'
...