Format

Send to

Choose Destination
J Cell Sci. 2014 Sep 15;127(Pt 18):3928-42. doi: 10.1242/jcs.143537. Epub 2014 Jul 11.

TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly.

Author information

1
Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA pradeep.uchil@yale.edu walther.mothes@yale.edu.
2
Department of Microbial Pathogenesis, Yale University School of Medicine, New Haven, CT 06536, USA.
3
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA.
4
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA.
5
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA Department of Biomedical Engineering, Yale University, New Haven, CT 06511, USA.
6
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520, USA Departments of Pharmacology and Yale Cancer Center, Yale University, New Haven, CT 06520, USA.

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 multi-adaptor 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.

KEYWORDS:

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

PMID:
25015296
PMCID:
PMC4163643
DOI:
10.1242/jcs.143537
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center