Mechanical force can enhance c-Src kinase activity by impairing autoinhibition.


Journal

Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626

Informations de publication

Date de publication:
01 03 2022
Historique:
received: 20 08 2021
revised: 21 12 2021
accepted: 28 01 2022
pubmed: 6 2 2022
medline: 15 4 2022
entrez: 5 2 2022
Statut: ppublish

Résumé

Cellular mechanosensing is pivotal for virtually all biological processes, and many molecular mechano-sensors and their way of function are being uncovered. In this work, we suggest that c-Src kinase acts as a direct mechano-sensor. c-Src is responsible for, among others, cell proliferation, and shows increased activity in stretched cells. In its native state, c-Src has little basal activity, because its kinase domain binds to an SH2 and SH3 domain. However, it is known that c-Src can bind to p130Cas, through which force can be transmitted to the membrane. Using molecular dynamics simulations, we show that force acting between the membrane-bound N-terminus of the SH3 domain and p130Cas induces partial SH3 unfolding, thereby impeding rebinding of the kinase domain onto SH2/SH3 and effectively enhancing kinase activity. Forces involved in this process are slightly lower or similar to the forces required to pull out c-Src from the membrane through the myristoyl linker, and key interactions involved in this anchoring are salt bridges between negative lipids and nearby basic residues in c-Src. Thus, c-Src appears to be a candidate for an intriguing mechanosensing mechanism of impaired kinase inhibition, which can be potentially tuned by membrane composition and other environmental factors.

Identifiants

pubmed: 35120901
pii: S0006-3495(22)00078-9
doi: 10.1016/j.bpj.2022.01.028
pmc: PMC8943751
pii:
doi:

Substances chimiques

Protein-Tyrosine Kinases EC 2.7.10.1
CSK Tyrosine-Protein Kinase EC 2.7.10.2

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

684-691

Informations de copyright

Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.

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Auteurs

Csaba Daday (C)

Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.

Svenja de Buhr (S)

Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.

Davide Mercadante (D)

Heidelberg Institute for Theoretical Studies, Heidelberg, Germany.

Frauke Gräter (F)

Heidelberg Institute for Theoretical Studies, Heidelberg, Germany; Interdisciplinary Center for Scientific Computing (IWR), Heidelberg University, Mathematikon, Heidelberg, Germany. Electronic address: frauke.graeter@h-its.org.

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Classifications MeSH