TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
Copyright policy )TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
Focal adhesions (FAs) are macromolecular complexes that connect the actin cytoskeleton to the extracellular matrix. Dynamic turnover of FAs is critical for cell migration. Paxillin is a multi-adaptor protein that plays an important role in regulating FA dynamics. Here, we identify TRIM15, a member of the TRIpartite Motif protein family, as a paxillin-interacting factor and a component of FAs. 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 FA proteins, TRIM15 is a stable FA component with restricted mobility due to its ability to form oligomers. TRIM15-depleted cells display impaired cell migration and FA disassembly rates in addition to enlarged FAs. Thus, our studies demonstrate a cellular function for TRIM15 as a regulatory component of FA turnover and cell migration.
- Yale University United States
Focal Adhesions, Intracellular Signaling Peptides and Proteins, Tripartite Motif Proteins, Kinetics, Mice, Protein Transport, Cell Movement, Histocompatibility Antigens, Animals, Humans, Paxillin, Carrier Proteins, Protein Binding
Focal Adhesions, Intracellular Signaling Peptides and Proteins, Tripartite Motif Proteins, Kinetics, Mice, Protein Transport, Cell Movement, Histocompatibility Antigens, Animals, Humans, Paxillin, Carrier Proteins, Protein Binding
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