---
_id: '10323'
abstract:
- lang: eng
  text: Molecular chaperones are central to cellular protein homeostasis. Dynamic
    disorder is a key feature of the complexes of molecular chaperones and their client
    proteins, and it facilitates the client release towards a folded state or the
    handover to downstream components. The dynamic nature also implies that a given
    chaperone can interact with many different client proteins, based on physico-chemical
    sequence properties rather than on structural complementarity of their (folded)
    3D structure. Yet, the balance between this promiscuity and some degree of client
    specificity is poorly understood. Here, we review recent atomic-level descriptions
    of chaperones with client proteins, including chaperones in complex with intrinsically
    disordered proteins, with membrane-protein precursors, or partially folded client
    proteins. We focus hereby on chaperone-client interactions that are independent
    of ATP. The picture emerging from these studies highlights the importance of dynamics
    in these complexes, whereby several interaction types, not only hydrophobic ones,
    contribute to the complex formation. We discuss these features of chaperone-client
    complexes and possible factors that may contribute to this balance of promiscuity
    and specificity.
acknowledgement: We thank Juan C. Fontecilla-Camps for insightful discussions related
  to ATP-driven machineries, and Elif Karagöz for providing the structural model of
  the Hsp90-Tau complex. This study was supported by the European Research Council
  (StG-2012-311318-ProtDyn2Function) and the Agence Nationale de la Recherche (ANR-18-CE92-0032-MitoMemProtImp).
article_number: '762005'
article_processing_charge: Yes (via OA deal)
article_type: original
author:
- first_name: Iva
  full_name: Sučec, Iva
  last_name: Sučec
- first_name: Beate
  full_name: Bersch, Beate
  last_name: Bersch
- first_name: Paul
  full_name: Schanda, Paul
  id: 7B541462-FAF6-11E9-A490-E8DFE5697425
  last_name: Schanda
  orcid: 0000-0002-9350-7606
citation:
  ama: Sučec I, Bersch B, Schanda P. How do chaperones bind (partly) unfolded client
    proteins? <i>Frontiers in Molecular Biosciences</i>. 2021;8. doi:<a href="https://doi.org/10.3389/fmolb.2021.762005">10.3389/fmolb.2021.762005</a>
  apa: Sučec, I., Bersch, B., &#38; Schanda, P. (2021). How do chaperones bind (partly)
    unfolded client proteins? <i>Frontiers in Molecular Biosciences</i>. Frontiers.
    <a href="https://doi.org/10.3389/fmolb.2021.762005">https://doi.org/10.3389/fmolb.2021.762005</a>
  chicago: Sučec, Iva, Beate Bersch, and Paul Schanda. “How Do Chaperones Bind (Partly)
    Unfolded Client Proteins?” <i>Frontiers in Molecular Biosciences</i>. Frontiers,
    2021. <a href="https://doi.org/10.3389/fmolb.2021.762005">https://doi.org/10.3389/fmolb.2021.762005</a>.
  ieee: I. Sučec, B. Bersch, and P. Schanda, “How do chaperones bind (partly) unfolded
    client proteins?,” <i>Frontiers in Molecular Biosciences</i>, vol. 8. Frontiers,
    2021.
  ista: Sučec I, Bersch B, Schanda P. 2021. How do chaperones bind (partly) unfolded
    client proteins? Frontiers in Molecular Biosciences. 8, 762005.
  mla: Sučec, Iva, et al. “How Do Chaperones Bind (Partly) Unfolded Client Proteins?”
    <i>Frontiers in Molecular Biosciences</i>, vol. 8, 762005, Frontiers, 2021, doi:<a
    href="https://doi.org/10.3389/fmolb.2021.762005">10.3389/fmolb.2021.762005</a>.
  short: I. Sučec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).
date_created: 2021-11-21T23:01:29Z
date_published: 2021-10-25T00:00:00Z
date_updated: 2023-08-14T11:55:04Z
day: '25'
ddc:
- '547'
department:
- _id: PaSc
doi: 10.3389/fmolb.2021.762005
external_id:
  isi:
  - '000717241700001'
  pmid:
  - '34760928'
file:
- access_level: open_access
  checksum: a5c9dbf80dc2c5aaa737f456c941d964
  content_type: application/pdf
  creator: cchlebak
  date_created: 2021-11-23T15:06:58Z
  date_updated: 2021-11-23T15:06:58Z
  file_id: '10333'
  file_name: 2021_FrontiersMolBioSc_Sučec.pdf
  file_size: 4700798
  relation: main_file
  success: 1
file_date_updated: 2021-11-23T15:06:58Z
has_accepted_license: '1'
intvolume: '         8'
isi: 1
language:
- iso: eng
license: https://creativecommons.org/licenses/by/4.0/
month: '10'
oa: 1
oa_version: Published Version
pmid: 1
publication: Frontiers in Molecular Biosciences
publication_identifier:
  eissn:
  - 2296-889X
publication_status: published
publisher: Frontiers
quality_controlled: '1'
scopus_import: '1'
status: public
title: How do chaperones bind (partly) unfolded client proteins?
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: 8
year: '2021'
...