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TRIP10

Domain

The F-BAR domain binds the phospholipid membrane with its concave surface. The end-to-end polymerization of dimers of these domains provides a curved surface that fits best membranes with around 600 A diameter, and may drive tubulation.

Function

Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL.

Post-translational modifications

Tyrosine phosphorylated. Also phosphorylated by PKA.

Sequence Similarities

Belongs to the FNBP1 family.

Tissue Specificity

Expressed in brain, colon, heart, kidney, liver, lung, megakaryocyte, ovary, pancreas, peripheral blood lymphocytes, placenta, prostate, skeletal muscle, small intestine, spleen, testis, thymus and trachea.

Cellular localization

Alternative names

CIP4, STOT, STP, TRIP10, Cdc42-interacting protein 4, Protein Felic, Salt tolerant protein, Thyroid receptor-interacting protein 10, hSTP, TR-interacting protein 10, TRIP-10

swissprot:Q15642 entrezGene:9322 omim:604504