0 673

Cited 38 times in

Vimentin filaments regulate integrin-ligand interactions by binding to the cytoplasmic tail of integrin β3.

Authors
 Jiyoon Kim  ;  Chansik Yang  ;  Eun Jin Kim  ;  Jungim Jang  ;  Se-Jong Kim  ;  So Min Kang  ;  Moon Gyo Kim  ;  Hosung Jung  ;  Dongeun Park  ;  Chungho Kim 
Citation
 JOURNAL OF CELL SCIENCE, Vol.129(10) : 2030-2042, 2016 
Journal Title
JOURNAL OF CELL SCIENCE
ISSN
 0021-9533 
Issue Date
2016
MeSH
Animals ; CHO Cells ; Cell Adhesion/genetics* ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Cell Movement/genetics ; Cricetinae ; Cricetulus ; Cytoskeleton/genetics ; Cytoskeleton/metabolism* ; Epithelial-Mesenchymal Transition/genetics ; Humans ; Integrin beta3/genetics* ; Integrin beta3/metabolism ; Ligands ; Protein Binding ; Protein Interaction Maps ; Proteomics ; Vimentin/genetics* ; Vimentin/metabolism
Keywords
H-Ras ; Integrin ; Integrin activation ; Talin ; Vimentin
Abstract
Vimentin, an intermediate filament protein induced during epithelial-to-mesenchymal transition, is known to regulate cell migration and invasion. However, it is still unclear how vimentin controls such behaviors. In this study, we aimed to find a new integrin regulator by investigating the H-Ras-mediated integrin suppression mechanism. Through a proteomic screen using the integrin β3 cytoplasmic tail protein, we found that vimentin might work as an effector of H-Ras signaling. H-Ras converted filamentous vimentin into aggregates near the nucleus, where no integrin binding can occur. In addition, an increase in the amount of vimentin filaments accessible to the integrin β3 tail enhanced talin-induced integrin binding to its ligands by inducing integrin clustering. In contrast, the vimentin head domain, which was found to bind directly to the integrin β3 tail and compete with endogenous vimentin filaments for integrin binding, induced nuclear accumulation of vimentin filaments and reduced the amount of integrin-ligand binding. Finally, we found that expression of the vimentin head domain can reduce cell migration and metastasis. From these data, we suggest that filamentous vimentin underneath the plasma membrane is involved in increasing integrin adhesiveness, and thus regulation of the vimentin-integrin interaction might control cell adhesion.
Full Text
http://jcs.biologists.org/content/129/10/2030.long
DOI
10.1242/jcs.180315
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Anatomy (해부학교실) > 1. Journal Papers
Yonsei Authors
Jung, Ho Sung(정호성) ORCID logo https://orcid.org/0000-0002-5059-8050
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/146941
사서에게 알리기
  feedback

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse

Links