TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Pradeep D. Uchil, Tobias Pawliczek, Tracy D. Reynolds, Siyuan Ding, Angelika Hinz, James B. Munro, Fang Huang, Robert W. Floyd, Haitao Yang, William L. Hamilton, Joerg Bewersdorf, Yong Xiong, David A. Calderwood, Walther Mothes

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Focal adhesions are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of focal adhesions is crucial for cell migration. Paxillin is a multiadaptor protein that plays an important role in regulating focal adhesion dynamics. Here, we identify TRIM15, a member of the tripartite motif protein family, as a paxillin-interacting factor and a component of focal adhesions. TRIM15 localizes to focal contacts in a myosin-II-independent manner by an interaction between its coiled-coil domain and the LD2 motif of paxillin. Unlike other focal adhesion proteins, TRIM15 is a stable focal adhesion component with restricted mobility due to its ability to form oligomers. TRIM15- depleted cells display impaired cell migration and reduced focal adhesion disassembly rates, in addition to enlarged focal adhesions. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of focal adhesion turnover and cell migration.

Original languageEnglish
Pages (from-to)3928-3942
Number of pages15
JournalJournal of cell science
Volume127
Issue number18
DOIs
StatePublished - 2014

Keywords

  • Cell migration
  • Focal adhesion disassembly
  • Focal adhesions
  • Paxillin
  • TRIM E3 ligases
  • TRIM15

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