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CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility.

Authors
  • Zhang, Mei
  • Liu, Jun
  • Cheng, Alan
  • Deyoung, Stephanie M
  • Chen, Xiaowei
  • Dold, Lisa H
  • Saltiel, Alan R
Type
Published Article
Journal
The EMBO journal
Publication Date
Nov 15, 2006
Volume
25
Issue
22
Pages
5284–5293
Identifiers
PMID: 17082770
Source
Medline
License
Unknown

Abstract

CAP/Ponsin belongs to the SoHo family of adaptor molecules that includes ArgBP2 and Vinexin. These proteins possess an N-terminal sorbin homology (SoHo) domain and three C-terminal SH3 domains that bind to diverse signaling molecules involved in a variety of cellular processes. Here, we show that CAP binds to the cytoskeletal proteins paxillin and vinculin. CAP localizes to cell-extracellular matrix (ECM) adhesion sites, and this process requires binding to vinculin. Overexpression of CAP induces the aggregation of paxillin, vinculin and actin at cell-ECM adhesion sites. Moreover, CAP inhibits adhesion-dependent processes such as cell spreading and focal adhesion turnover, whereas a CAP mutant that is unable to localize to cell-ECM adhesion sites is incapable of exerting these effects. Finally, depletion of CAP by siRNA-mediated knockdown leads to enhanced cell spreading, migration and the activation of the PAK/MEK/ERK pathway in REF52 cells. Taken together, these results indicate that CAP is a cytoskeletal adaptor protein involved in modulating adhesion-mediated signaling events that lead to cell migration.

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