The mechanical response of talin

Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing d...

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Main Authors:	Yao, Mingxi, Goult, Benjamin T., Klapholz, Benjamin, Hu, Xian, Toseland, Christopher P., Guo, Yingjian, Cong, Peiwen, Sheetz, Michael P., Yan, Jie
Format:	Online
Language:	English
Published:	Nature Publishing Group 2016
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941051/

id	pubmed-4941051
recordtype	oai_dc
spelling	pubmed-49410512016-09-06 The mechanical response of talin Yao, Mingxi Goult, Benjamin T. Klapholz, Benjamin Hu, Xian Toseland, Christopher P. Guo, Yingjian Cong, Peiwen Sheetz, Michael P. Yan, Jie Article Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway. Nature Publishing Group 2016-07-07 /pmc/articles/PMC4941051/ /pubmed/27384267 http://dx.doi.org/10.1038/ncomms11966 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Yao, Mingxi Goult, Benjamin T. Klapholz, Benjamin Hu, Xian Toseland, Christopher P. Guo, Yingjian Cong, Peiwen Sheetz, Michael P. Yan, Jie
spellingShingle	Yao, Mingxi Goult, Benjamin T. Klapholz, Benjamin Hu, Xian Toseland, Christopher P. Guo, Yingjian Cong, Peiwen Sheetz, Michael P. Yan, Jie The mechanical response of talin
author_facet	Yao, Mingxi Goult, Benjamin T. Klapholz, Benjamin Hu, Xian Toseland, Christopher P. Guo, Yingjian Cong, Peiwen Sheetz, Michael P. Yan, Jie
author_sort	Yao, Mingxi
title	The mechanical response of talin
title_short	The mechanical response of talin
title_full	The mechanical response of talin
title_fullStr	The mechanical response of talin
title_full_unstemmed	The mechanical response of talin
title_sort	mechanical response of talin
description	Talin, a force-bearing cytoplasmic adapter essential for integrin-mediated cell adhesion, links the actin cytoskeleton to integrin-based cell–extracellular matrix adhesions at the plasma membrane. Its C-terminal rod domain, which contains 13 helical bundles, plays important roles in mechanosensing during cell adhesion and spreading. However, how the structural stability and transition kinetics of the 13 helical bundles of talin are utilized in the diverse talin-dependent mechanosensing processes remains poorly understood. Here we report the force-dependent unfolding and refolding kinetics of all talin rod domains. Using experimentally determined kinetics parameters, we determined the dynamics of force fluctuation during stretching of talin under physiologically relevant pulling speeds and experimentally measured extension fluctuation trajectories. Our results reveal that force-dependent stochastic unfolding and refolding of talin rod domains make talin a very effective force buffer that sets a physiological force range of only a few pNs in the talin-mediated force transmission pathway.
publisher	Nature Publishing Group
publishDate	2016
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4941051/
_version_	1613607545901940736

The mechanical response of talin

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