Vimentin filament controls integrin α5β1-mediated cell adhesion by binding to integrin through its Ser38 residue.

Abstract:

:Regulation of integrin affinity for its ligand is essential for cell adhesion and migration. Here, we found that direct interaction of vimentin with integrin β1 can enhance binding of integrin α5β1 to its ligand, fibronectin. Conversely, blocking the interaction reduced fibronectin binding, cell migration on a fibronectin-coated surface, and neural tube closure during Xenopus embryogenesis. We also found that withaferin A (WFA), a natural compound known to inhibit vimentin function, can suppress the vimentin-integrin interaction and abolish fibronectin binding. Finally, we identified Ser38 of vimentin as a critical residue for integrin binding. Our results suggest that phosphorylation of vimentin at Ser38 may regulate the integrin-ligand interaction, thus providing a molecular basis for antivimentin therapeutic strategies.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Kim J,Jang J,Yang C,Kim EJ,Jung H,Kim C

doi

10.1002/1873-3468.12430

subject

Has Abstract

pub_date

2016-10-01 00:00:00

pages

3517-3525

issue

20

eissn

0014-5793

issn

1873-3468

journal_volume

590

pub_type

信件
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    doi:10.1016/j.febslet.2006.12.029

    authors: El Sayegh TY,Kapus A,McCulloch CA

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    doi:10.1016/j.febslet.2007.03.038

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    更新日期:2016-02-01 00:00:00