Talin is required to increase stiffness of focal molecular complex in its early formation process.


Journal

Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516

Informations de publication

Date de publication:
20 10 2019
Historique:
received: 09 08 2019
accepted: 15 08 2019
pubmed: 28 8 2019
medline: 9 6 2020
entrez: 28 8 2019
Statut: ppublish

Résumé

For cellular adaptation in mechanical environments, it is important to consider transmission of forces from the outside to the inside of cells via a focal molecular complex. The focal molecular complex, which consists of integrin, talin, vinculin and actin, is known to form in response to a force applied via the extra-cellular matrix (ECM). In the early formation process of the complex, the complex-actin connection is reinforced. These structural changes of the nascent complex result in an increase in its mechanical integrity and overall stiffness, possibly leading to the maturation of the nascent complex by enhancing force transmission. In this study, we hypothesized that the complex component talin is a crucial factor in increasing the stiffness of the nascent complex. To test the hypothesis, we used atomic force microscopy (AFM) to measure the stiffness of the nascent complex using a probe coated with fibronectin. Stiffness measurements were conducted for intact and talin knocked-down cells. Our results demonstrated that talin was required to increase the stiffness of the nascent complex, which could be caused by the reinforced connection between the complex and actin filaments mediated by talin.

Identifiants

pubmed: 31451222
pii: S0006-291X(19)31614-6
doi: 10.1016/j.bbrc.2019.08.091
pii:
doi:

Substances chimiques

Actins 0
Fibronectins 0
Integrins 0
Talin 0
Tln1 protein, mouse 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

579-583

Informations de copyright

Copyright © 2019 Elsevier Inc. All rights reserved.

Auteurs

Nobuhiko Nakao (N)

Department of Micro Engineering, Graduate School of Engineering, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan; Institute for Frontier Life and Mechanical Sciences, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan.

Koichiro Maki (K)

Helsinki Institute of Life Science, University of Helsinki, Haartmaninkatu 8, Helsinki, FI00290, Finland; Department of Mechanical Engineering, Graduate School of Engineering, The University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo, 113-8656, Japan.

Mohammad R K Mofrad (MRK)

Department of Bioengineering, University of California, Berkeley, CA94720, USA; Department of Mechanical Engineering, University of California, Berkeley, CA94720-1762, USA; Molecular Biophysics and Integrative Bioimaging Division, Lawrence Berkeley National Lab, CA94720, Berkeley, USA.

Taiji Adachi (T)

Department of Micro Engineering, Graduate School of Engineering, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan; Institute for Frontier Life and Mechanical Sciences, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan; Department of Mammalian Regulatory Network, Graduate School of Biostudies, Kyoto University, 53 Shogoin Kawahara-cho, Sakyo, Kyoto, 606-8507, Japan. Electronic address: adachi@infront.kyoto-u.ac.jp.

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