---
_id: '10705'
abstract:
- lang: eng
  text: Although rigidity and jamming transitions have been widely studied in physics
    and material science, their importance in a number of biological processes, including
    embryo development, tissue homeostasis, wound healing, and disease progression,
    has only begun to be recognized in the past few years. The hypothesis that biological
    systems can undergo rigidity/jamming transitions is attractive, as it would allow
    these systems to change their material properties rapidly and strongly. However,
    whether such transitions indeed occur in biological systems, how they are being
    regulated, and what their physiological relevance might be, is still being debated.
    Here, we review theoretical and experimental advances from the past few years,
    focusing on the regulation and role of potential tissue rigidity transitions in
    different biological processes.
acknowledgement: We thank present and former members of the Heisenberg and Hannezo
  groups, in particular Bernat Corominas-Murtra and Nicoletta Petridou, for helpful
  discussions, and Claudia Flandoli for the artwork. We apologize for not being able
  to cite a number of highly relevant studies, to stay within the maximum allowed
  number of citations.
article_processing_charge: No
article_type: original
author:
- first_name: Edouard B
  full_name: Hannezo, Edouard B
  id: 3A9DB764-F248-11E8-B48F-1D18A9856A87
  last_name: Hannezo
  orcid: 0000-0001-6005-1561
- 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: Hannezo EB, Heisenberg C-PJ. Rigidity transitions in development and disease.
    <i>Trends in Cell Biology</i>. 2022;32(5):P433-444. doi:<a href="https://doi.org/10.1016/j.tcb.2021.12.006">10.1016/j.tcb.2021.12.006</a>
  apa: Hannezo, E. B., &#38; Heisenberg, C.-P. J. (2022). Rigidity transitions in
    development and disease. <i>Trends in Cell Biology</i>. Cell Press. <a href="https://doi.org/10.1016/j.tcb.2021.12.006">https://doi.org/10.1016/j.tcb.2021.12.006</a>
  chicago: Hannezo, Edouard B, and Carl-Philipp J Heisenberg. “Rigidity Transitions
    in Development and Disease.” <i>Trends in Cell Biology</i>. Cell Press, 2022.
    <a href="https://doi.org/10.1016/j.tcb.2021.12.006">https://doi.org/10.1016/j.tcb.2021.12.006</a>.
  ieee: E. B. Hannezo and C.-P. J. Heisenberg, “Rigidity transitions in development
    and disease,” <i>Trends in Cell Biology</i>, vol. 32, no. 5. Cell Press, pp. P433-444,
    2022.
  ista: Hannezo EB, Heisenberg C-PJ. 2022. Rigidity transitions in development and
    disease. Trends in Cell Biology. 32(5), P433-444.
  mla: Hannezo, Edouard B., and Carl-Philipp J. Heisenberg. “Rigidity Transitions
    in Development and Disease.” <i>Trends in Cell Biology</i>, vol. 32, no. 5, Cell
    Press, 2022, pp. P433-444, doi:<a href="https://doi.org/10.1016/j.tcb.2021.12.006">10.1016/j.tcb.2021.12.006</a>.
  short: E.B. Hannezo, C.-P.J. Heisenberg, Trends in Cell Biology 32 (2022) P433-444.
date_created: 2022-01-30T23:01:34Z
date_published: 2022-05-01T00:00:00Z
date_updated: 2023-08-02T14:03:53Z
day: '01'
department:
- _id: EdHa
- _id: CaHe
doi: 10.1016/j.tcb.2021.12.006
external_id:
  isi:
  - '000795773900009'
  pmid:
  - '35058104'
intvolume: '        32'
isi: 1
issue: '5'
language:
- iso: eng
month: '05'
oa_version: None
page: P433-444
pmid: 1
publication: Trends in Cell Biology
publication_identifier:
  eissn:
  - 1879-3088
  issn:
  - 0962-8924
publication_status: published
publisher: Cell Press
quality_controlled: '1'
scopus_import: '1'
status: public
title: Rigidity transitions in development and disease
type: journal_article
user_id: 4359f0d1-fa6c-11eb-b949-802e58b17ae8
volume: 32
year: '2022'
...
---
_id: '11051'
abstract:
- lang: eng
  text: Nuclear pore complexes (NPCs) bridge the nucleus and the cytoplasm and are
    indispensable for crucial cellular activities, such as bidirectional molecular
    trafficking and gene transcription regulation. The discovery of long-lived proteins
    (LLPs) in NPCs from postmitotic cells raises the exciting possibility that the
    maintenance of NPC integrity might play an inherent role in lifelong cell function.
    Age-dependent deterioration of NPCs and loss of nuclear integrity have been linked
    to age-related decline in postmitotic cell function and degenerative diseases.
    In this review, we discuss our current understanding of NPC maintenance in proliferating
    and postmitotic cells, and how malfunction of nucleoporins (Nups) might contribute
    to the pathogenesis of various neurodegenerative and cardiovascular diseases.
article_processing_charge: No
article_type: review
author:
- first_name: Jinqiang
  full_name: Liu, Jinqiang
  last_name: Liu
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
citation:
  ama: Liu J, Hetzer M. Nuclear pore complex maintenance and implications for age-related
    diseases. <i>Trends in Cell Biology</i>. 2022;32(3):P216-227. doi:<a href="https://doi.org/10.1016/j.tcb.2021.10.001">10.1016/j.tcb.2021.10.001</a>
  apa: Liu, J., &#38; Hetzer, M. (2022). Nuclear pore complex maintenance and implications
    for age-related diseases. <i>Trends in Cell Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.tcb.2021.10.001">https://doi.org/10.1016/j.tcb.2021.10.001</a>
  chicago: Liu, Jinqiang, and Martin Hetzer. “Nuclear Pore Complex Maintenance and
    Implications for Age-Related Diseases.” <i>Trends in Cell Biology</i>. Elsevier,
    2022. <a href="https://doi.org/10.1016/j.tcb.2021.10.001">https://doi.org/10.1016/j.tcb.2021.10.001</a>.
  ieee: J. Liu and M. Hetzer, “Nuclear pore complex maintenance and implications for
    age-related diseases,” <i>Trends in Cell Biology</i>, vol. 32, no. 3. Elsevier,
    pp. P216-227, 2022.
  ista: Liu J, Hetzer M. 2022. Nuclear pore complex maintenance and implications for
    age-related diseases. Trends in Cell Biology. 32(3), P216-227.
  mla: Liu, Jinqiang, and Martin Hetzer. “Nuclear Pore Complex Maintenance and Implications
    for Age-Related Diseases.” <i>Trends in Cell Biology</i>, vol. 32, no. 3, Elsevier,
    2022, pp. P216-227, doi:<a href="https://doi.org/10.1016/j.tcb.2021.10.001">10.1016/j.tcb.2021.10.001</a>.
  short: J. Liu, M. Hetzer, Trends in Cell Biology 32 (2022) P216-227.
date_created: 2022-04-07T07:43:01Z
date_published: 2022-03-01T00:00:00Z
date_updated: 2022-07-18T08:58:33Z
day: '01'
doi: 10.1016/j.tcb.2021.10.001
extern: '1'
external_id:
  pmid:
  - '34782239'
intvolume: '        32'
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '03'
oa_version: None
page: P216-227
pmid: 1
publication: Trends in Cell Biology
publication_identifier:
  issn:
  - 0962-8924
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Nuclear pore complex maintenance and implications for age-related diseases
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 32
year: '2022'
...
---
_id: '11083'
abstract:
- lang: eng
  text: Nuclear pore complex (NPC) proteins are known for their critical roles in
    regulating nucleocytoplasmic traffic of macromolecules across the nuclear envelope.
    However, recent findings suggest that some nucleoporins (Nups), including Nup98,
    have additional functions in developmental gene regulation. Nup98, which exhibits
    transcription-dependent mobility at the NPC but can also bind chromatin away from
    the nuclear envelope, is frequently involved in chromosomal translocations in
    a subset of patients suffering from acute myeloid leukemia (AML). A common paradigm
    suggests that Nup98 translocations cause aberrant transcription when they are
    recuited to aberrant genomic loci. Importantly, this model fails to account for
    the potential loss of wild type (WT) Nup98 function in the presence of Nup98 translocation
    mutants. Here we examine how the cell might regulate Nup98 nucleoplasmic protein
    levels to control transcription in healthy cells. In addition, we discuss the
    possibility that dominant negative Nup98 fusion proteins disrupt the transcriptional
    activity of WT Nup98 in the nucleoplasm to drive AML.
article_processing_charge: No
article_type: letter_note
author:
- first_name: Tobias M.
  full_name: Franks, Tobias M.
  last_name: Franks
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
citation:
  ama: Franks TM, Hetzer M. The role of Nup98 in transcription regulation in healthy
    and diseased cells. <i>Trends in Cell Biology</i>. 2013;23(3):112-117. doi:<a
    href="https://doi.org/10.1016/j.tcb.2012.10.013">10.1016/j.tcb.2012.10.013</a>
  apa: Franks, T. M., &#38; Hetzer, M. (2013). The role of Nup98 in transcription
    regulation in healthy and diseased cells. <i>Trends in Cell Biology</i>. Elsevier.
    <a href="https://doi.org/10.1016/j.tcb.2012.10.013">https://doi.org/10.1016/j.tcb.2012.10.013</a>
  chicago: Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription
    Regulation in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>. Elsevier,
    2013. <a href="https://doi.org/10.1016/j.tcb.2012.10.013">https://doi.org/10.1016/j.tcb.2012.10.013</a>.
  ieee: T. M. Franks and M. Hetzer, “The role of Nup98 in transcription regulation
    in healthy and diseased cells,” <i>Trends in Cell Biology</i>, vol. 23, no. 3.
    Elsevier, pp. 112–117, 2013.
  ista: Franks TM, Hetzer M. 2013. The role of Nup98 in transcription regulation in
    healthy and diseased cells. Trends in Cell Biology. 23(3), 112–117.
  mla: Franks, Tobias M., and Martin Hetzer. “The Role of Nup98 in Transcription Regulation
    in Healthy and Diseased Cells.” <i>Trends in Cell Biology</i>, vol. 23, no. 3,
    Elsevier, 2013, pp. 112–17, doi:<a href="https://doi.org/10.1016/j.tcb.2012.10.013">10.1016/j.tcb.2012.10.013</a>.
  short: T.M. Franks, M. Hetzer, Trends in Cell Biology 23 (2013) 112–117.
date_created: 2022-04-07T07:50:33Z
date_published: 2013-03-01T00:00:00Z
date_updated: 2022-07-18T08:45:34Z
day: '01'
doi: 10.1016/j.tcb.2012.10.013
extern: '1'
external_id:
  pmid:
  - '23246429'
intvolume: '        23'
issue: '3'
keyword:
- Cell Biology
language:
- iso: eng
month: '03'
oa_version: None
page: 112-117
pmid: 1
publication: Trends in Cell Biology
publication_identifier:
  issn:
  - 0962-8924
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: The role of Nup98 in transcription regulation in healthy and diseased cells
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 23
year: '2013'
...
---
_id: '11110'
abstract:
- lang: eng
  text: Nuclear pore complexes are large aqueous channels that penetrate the nuclear
    envelope, thereby connecting the nuclear interior with the cytoplasm. Until recently,
    these macromolecular complexes were viewed as static structures, the only function
    of which was to control the molecular trafficking between the two compartments.
    It has now become evident that this simplistic scenario is inaccurate and that
    nuclear pore complexes are highly dynamic multiprotein assemblies involved in
    diverse cellular processes ranging from the organization of the cytoskeleton to
    gene expression. In this review, we discuss the most recent developments in the
    nuclear-pore-complex field, focusing on the assembly, disassembly, maintenance
    and function of this macromolecular structure.
article_processing_charge: No
article_type: review
author:
- first_name: Maximiliano A.
  full_name: D’Angelo, Maximiliano A.
  last_name: D’Angelo
- first_name: Martin W
  full_name: HETZER, Martin W
  id: 86c0d31b-b4eb-11ec-ac5a-eae7b2e135ed
  last_name: HETZER
  orcid: 0000-0002-2111-992X
citation:
  ama: D’Angelo MA, Hetzer M. Structure, dynamics and function of nuclear pore complexes.
    <i>Trends in Cell Biology</i>. 2008;18(10):456-466. doi:<a href="https://doi.org/10.1016/j.tcb.2008.07.009">10.1016/j.tcb.2008.07.009</a>
  apa: D’Angelo, M. A., &#38; Hetzer, M. (2008). Structure, dynamics and function
    of nuclear pore complexes. <i>Trends in Cell Biology</i>. Elsevier. <a href="https://doi.org/10.1016/j.tcb.2008.07.009">https://doi.org/10.1016/j.tcb.2008.07.009</a>
  chicago: D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function
    of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>. Elsevier, 2008. <a
    href="https://doi.org/10.1016/j.tcb.2008.07.009">https://doi.org/10.1016/j.tcb.2008.07.009</a>.
  ieee: M. A. D’Angelo and M. Hetzer, “Structure, dynamics and function of nuclear
    pore complexes,” <i>Trends in Cell Biology</i>, vol. 18, no. 10. Elsevier, pp.
    456–466, 2008.
  ista: D’Angelo MA, Hetzer M. 2008. Structure, dynamics and function of nuclear pore
    complexes. Trends in Cell Biology. 18(10), 456–466.
  mla: D’Angelo, Maximiliano A., and Martin Hetzer. “Structure, Dynamics and Function
    of Nuclear Pore Complexes.” <i>Trends in Cell Biology</i>, vol. 18, no. 10, Elsevier,
    2008, pp. 456–66, doi:<a href="https://doi.org/10.1016/j.tcb.2008.07.009">10.1016/j.tcb.2008.07.009</a>.
  short: M.A. D’Angelo, M. Hetzer, Trends in Cell Biology 18 (2008) 456–466.
date_created: 2022-04-07T07:55:10Z
date_published: 2008-10-01T00:00:00Z
date_updated: 2022-07-18T08:55:33Z
day: '01'
doi: 10.1016/j.tcb.2008.07.009
extern: '1'
external_id:
  pmid:
  - '18786826'
intvolume: '        18'
issue: '10'
keyword:
- Cell Biology
language:
- iso: eng
month: '10'
oa_version: None
page: 456-466
pmid: 1
publication: Trends in Cell Biology
publication_identifier:
  issn:
  - 0962-8924
publication_status: published
publisher: Elsevier
quality_controlled: '1'
scopus_import: '1'
status: public
title: Structure, dynamics and function of nuclear pore complexes
type: journal_article
user_id: 72615eeb-f1f3-11ec-aa25-d4573ddc34fd
volume: 18
year: '2008'
...