Coupling of vinculin to F-actin demands Syndecan-4 proteoglycan

Coupling of vinculin to F-actin demands Syndecan-4 proteoglycan

Author Cavalheiro, R. P. Autor UNIFESP Google Scholar
Lima, M. A. Autor UNIFESP Google Scholar
Jarrouge-Boucas, T. R. Autor UNIFESP Google Scholar
Viana, G. M. Autor UNIFESP Google Scholar
Lopes, C. C. Autor UNIFESP Google Scholar
Coulson-Thomas, V. J. Autor UNIFESP Google Scholar
Dreyfuss, J. L. Autor UNIFESP Google Scholar
Yates, E. A. Autor UNIFESP Google Scholar
Tersariol, I. L. S. Autor UNIFESP Google Scholar
Nader, H. B. Autor UNIFESP Google Scholar
Abstract Syndecans are heparan sulfate proteoglycans characterized as transmembrane receptors that act cooperatively with the cell surface and extracellular matrix proteins. Syn4 knockdown was performed in orderto address its role in endothelial cells (EC) behavior. Normal EC and shRNA-Syn4-EC cells were studied comparatively using complementary confocal, super-resolution and non-linear microscopic techniques. Confocal and super-resolution microscopy revealed that Syn4 knockdown alters the level and arrangement of essential proteins for focal adhesion, evidenced by the decoupling of vinculin from F-actin filaments. Furthermore, Syn4 knockdown alters the actin network leading to filopodial protrusions connected by VE-cadherin rich junction. shRNA-Syn4-EC showed reduced adhesion and increased migration. Also, Syn4 silencing alters cell cycle as well as cell proliferation. Moreover, the ability of EC to form tube-like structures in matrigel is reduced when Syn4 is silenced. Together, the results suggest a mechanism in which Syndecan-4 acts as a central mediator that bridges fibronectin, integrin and intracellular components (actin and vinculin) and once silenced, the cytoskeleton protein network is disrupted. Ultimately, the results highlight Syn4 relevance for balanced cell behavior. (C) 2016 Elsevier B.V. All rights reserved.
Keywords Heparan sulfate
beta 1 integrin
Focal adhesion proteins
Super-resolution microscopy
Actin network
xmlui.dri2xhtml.METS-1.0.item-coverage Amsterdam
Language English
Sponsor CAPES (Coordenagdo de Aperfeicoamento de Pessoal de Nivel Superior)
CNPq (Conselho Nacional de Desenvolvimento Cientffico e Tecnologico)
FAPESP (Fundacao de Amparo a Pesquisa do Estado de sao Paulo), Brazil
Grant number FAPESP: 15/08782-3
FAPESP: 15/03964-6
Date 2017
Published in Matrix Biology. Amsterdam, v. 63, p. 23-37, 2017.
ISSN 0945-053X (Sherpa/Romeo, impact factor)
Publisher Elsevier Science Bv
Extent 23-37
Access rights Closed access
Type Article
Web of Science ID WOS:000413135300003

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