Growth factor dependent changes in nanoscale architecture of focal adhesions

Abstract Focal adhesions (FAs) are flat elongated structures that mediate cell migration and link the cytoskeleton to the extracellular matrix. Along the vertical axis FAs were shown to be composed of three layers. We used structured illumination microscopy to examine the longitudinal distribution o...

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Autores principales:	Karin Legerstee, Tsion E. Abraham, Wiggert A. van Cappellen, Alex L. Nigg, Johan A. Slotman, Adriaan B. Houtsmuller
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/04042c18fbe1426ea391cb28c528894f
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spelling	oai:doaj.org-article:04042c18fbe1426ea391cb28c528894f2021-12-02T14:16:17ZGrowth factor dependent changes in nanoscale architecture of focal adhesions10.1038/s41598-021-81898-x2045-2322https://doaj.org/article/04042c18fbe1426ea391cb28c528894f2021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-81898-xhttps://doaj.org/toc/2045-2322Abstract Focal adhesions (FAs) are flat elongated structures that mediate cell migration and link the cytoskeleton to the extracellular matrix. Along the vertical axis FAs were shown to be composed of three layers. We used structured illumination microscopy to examine the longitudinal distribution of four hallmark FA proteins, which we also used as markers for these layers. At the FA ends pointing towards the adherent membrane edge (heads), bottom layer protein paxillin protruded, while at the opposite ends (tails) intermediate layer protein vinculin and top layer proteins zyxin and VASP extended further. At the tail tips, only intermediate layer protein vinculin protruded. Importantly, head and tail compositions were altered during HGF-induced scattering with paxillin heads being shorter and zyxin tails longer. Additionally, FAs at protruding or retracting membrane edges had longer paxillin heads than FAs at static edges. These data suggest that redistribution of FA-proteins with respect to each other along FAs is involved in cell movement.Karin LegersteeTsion E. AbrahamWiggert A. van CappellenAlex L. NiggJohan A. SlotmanAdriaan B. HoutsmullerNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Karin Legerstee Tsion E. Abraham Wiggert A. van Cappellen Alex L. Nigg Johan A. Slotman Adriaan B. Houtsmuller Growth factor dependent changes in nanoscale architecture of focal adhesions
description	Abstract Focal adhesions (FAs) are flat elongated structures that mediate cell migration and link the cytoskeleton to the extracellular matrix. Along the vertical axis FAs were shown to be composed of three layers. We used structured illumination microscopy to examine the longitudinal distribution of four hallmark FA proteins, which we also used as markers for these layers. At the FA ends pointing towards the adherent membrane edge (heads), bottom layer protein paxillin protruded, while at the opposite ends (tails) intermediate layer protein vinculin and top layer proteins zyxin and VASP extended further. At the tail tips, only intermediate layer protein vinculin protruded. Importantly, head and tail compositions were altered during HGF-induced scattering with paxillin heads being shorter and zyxin tails longer. Additionally, FAs at protruding or retracting membrane edges had longer paxillin heads than FAs at static edges. These data suggest that redistribution of FA-proteins with respect to each other along FAs is involved in cell movement.
format	article
author	Karin Legerstee Tsion E. Abraham Wiggert A. van Cappellen Alex L. Nigg Johan A. Slotman Adriaan B. Houtsmuller
author_facet	Karin Legerstee Tsion E. Abraham Wiggert A. van Cappellen Alex L. Nigg Johan A. Slotman Adriaan B. Houtsmuller
author_sort	Karin Legerstee
title	Growth factor dependent changes in nanoscale architecture of focal adhesions
title_short	Growth factor dependent changes in nanoscale architecture of focal adhesions
title_full	Growth factor dependent changes in nanoscale architecture of focal adhesions
title_fullStr	Growth factor dependent changes in nanoscale architecture of focal adhesions
title_full_unstemmed	Growth factor dependent changes in nanoscale architecture of focal adhesions
title_sort	growth factor dependent changes in nanoscale architecture of focal adhesions
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/04042c18fbe1426ea391cb28c528894f
work_keys_str_mv	AT karinlegerstee growthfactordependentchangesinnanoscalearchitectureoffocaladhesions AT tsioneabraham growthfactordependentchangesinnanoscalearchitectureoffocaladhesions AT wiggertavancappellen growthfactordependentchangesinnanoscalearchitectureoffocaladhesions AT alexlnigg growthfactordependentchangesinnanoscalearchitectureoffocaladhesions AT johanaslotman growthfactordependentchangesinnanoscalearchitectureoffocaladhesions AT adriaanbhoutsmuller growthfactordependentchangesinnanoscalearchitectureoffocaladhesions
_version_	1718391645508993024

Growth factor dependent changes in nanoscale architecture of focal adhesions

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