TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly | Zendy

Pradeep D. Uchil | Zendy; Tobias Pawliczek | Zendy; Tracy Reynolds | Zendy; Siyuan Ding | Zendy; Angelika Hinz | Zendy; James B. Munro | Zendy; Fang Huang | Zendy; Warren Floyd | Zendy; Haitao Yang | Zendy; William L. Hamilton | Zendy; Joerg Bewersdorf | Zendy; Yong Xiong | Zendy; David Calderwood | Zendy; Walther Mothes | Zendy

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TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly

Author(s) -

Pradeep D. Uchil,

Tobias Pawliczek,

Tracy Reynolds,

Siyuan Ding,

Angelika Hinz,

James B. Munro,

Fang Huang,

Warren Floyd,

Haitao Yang,

William L. Hamilton,

Joerg Bewersdorf,

Yong Xiong,

David Calderwood,

Walther Mothes

Publication year - 2014

Publication title -

journal of cell science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.384

H-Index - 278

eISSN - 1477-9137

pISSN - 0021-9533

DOI - 10.1242/jcs.143537

Subject(s) - focal adhesion , paxillin , ptk2 , microbiology and biotechnology , biology , extracellular matrix , lim domain , cell adhesion , vinculin , integrin , cytoskeleton , actin cytoskeleton , cell migration , focal point , myosin , signal transducing adaptor protein , actin , cardinal point , cell , signal transduction , biochemistry , transcription factor , mitogen activated protein kinase kinase , protein kinase c , gene , physics , optics , zinc finger

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.

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