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Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation

Transduction of extracellular matrix mechanics affects cell migration, proliferation, and differentiation. While this mechanotransduction is known to depend on the regulation of focal adhesion kinase phosphorylation on Y397 (FAKpY397), the mechanism remains elusive. To address this, we developed a m...

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Autores principales: Cheng, Bo, Wan, Wanting, Huang, Guoyou, Li, Yuhui, Genin, Guy M., Mofrad, Mohammad R. K., Lu, Tian Jian, Xu, Feng, Lin, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056303/
https://www.ncbi.nlm.nih.gov/pubmed/32181337
http://dx.doi.org/10.1126/sciadv.aax1909
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author Cheng, Bo
Wan, Wanting
Huang, Guoyou
Li, Yuhui
Genin, Guy M.
Mofrad, Mohammad R. K.
Lu, Tian Jian
Xu, Feng
Lin, Min
author_facet Cheng, Bo
Wan, Wanting
Huang, Guoyou
Li, Yuhui
Genin, Guy M.
Mofrad, Mohammad R. K.
Lu, Tian Jian
Xu, Feng
Lin, Min
author_sort Cheng, Bo
collection PubMed
description Transduction of extracellular matrix mechanics affects cell migration, proliferation, and differentiation. While this mechanotransduction is known to depend on the regulation of focal adhesion kinase phosphorylation on Y397 (FAKpY397), the mechanism remains elusive. To address this, we developed a mathematical model to test the hypothesis that FAKpY397-based mechanosensing arises from the dynamics of nanoscale integrin clustering, stiffness-dependent disassembly of integrin clusters, and FAKY397 phosphorylation within integrin clusters. Modeling results predicted that integrin clustering dynamics governs how cells convert substrate stiffness to FAKpY397, and hence governs how different cell types transduce mechanical signals. Existing experiments on MDCK cells and HT1080 cells, as well as our new experiments on 3T3 fibroblasts, confirmed our predictions and supported our model. Our results suggest a new pathway by which integrin clusters enable cells to calibrate responses to their mechanical microenvironment.
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spelling pubmed-70563032020-03-16 Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation Cheng, Bo Wan, Wanting Huang, Guoyou Li, Yuhui Genin, Guy M. Mofrad, Mohammad R. K. Lu, Tian Jian Xu, Feng Lin, Min Sci Adv Research Articles Transduction of extracellular matrix mechanics affects cell migration, proliferation, and differentiation. While this mechanotransduction is known to depend on the regulation of focal adhesion kinase phosphorylation on Y397 (FAKpY397), the mechanism remains elusive. To address this, we developed a mathematical model to test the hypothesis that FAKpY397-based mechanosensing arises from the dynamics of nanoscale integrin clustering, stiffness-dependent disassembly of integrin clusters, and FAKY397 phosphorylation within integrin clusters. Modeling results predicted that integrin clustering dynamics governs how cells convert substrate stiffness to FAKpY397, and hence governs how different cell types transduce mechanical signals. Existing experiments on MDCK cells and HT1080 cells, as well as our new experiments on 3T3 fibroblasts, confirmed our predictions and supported our model. Our results suggest a new pathway by which integrin clusters enable cells to calibrate responses to their mechanical microenvironment. American Association for the Advancement of Science 2020-03-04 /pmc/articles/PMC7056303/ /pubmed/32181337 http://dx.doi.org/10.1126/sciadv.aax1909 Text en Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). http://creativecommons.org/licenses/by-nc/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (http://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited.
spellingShingle Research Articles
Cheng, Bo
Wan, Wanting
Huang, Guoyou
Li, Yuhui
Genin, Guy M.
Mofrad, Mohammad R. K.
Lu, Tian Jian
Xu, Feng
Lin, Min
Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title_full Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title_fullStr Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title_full_unstemmed Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title_short Nanoscale integrin cluster dynamics controls cellular mechanosensing via FAKY397 phosphorylation
title_sort nanoscale integrin cluster dynamics controls cellular mechanosensing via faky397 phosphorylation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7056303/
https://www.ncbi.nlm.nih.gov/pubmed/32181337
http://dx.doi.org/10.1126/sciadv.aax1909
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