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FBP17 and CIP4 prime the membrane of resting cells for fast endophilin-mediated endocytosis by recruiting the 5'-lipid phosphatase SHIP2 and lamellipodin to mediate the local production of phosphatidylinositol-3,4-bisphosphate and endophilin pre-enrichment.
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Results suggest that FBP17 is highly expressed in breast cancer cells and facilitates the invasion of breast cancer cells.
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FBP17 is the local activator of actin polymerization that is inhibited by PM tension in the feedback loop that regulates cell migration.
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Knockdown of PSTPIP2 inmacrophages enhances the assembly of FBP17, leading to'hyperactivation' of actin nucleation at podosomes and ECM degradation.
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F-BAR protein Rapostlin, whose activity is regulated by Rnd2, plays a key role in spine formation through the regulation of membrane dynamics.
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Results suggest a functional link between FBP17-dependent membrane tubulation and clathrin-dependent budding. Clathrin spatially directs membrane invaginations that lead to the generation of endocytic vesicles larger than those enclosed by the coat.
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co-immunoprecipitation of endogenous proteins in 293T cells confirms physiological relevance of TNKS as interaction partner of FBP17
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FBP17 interacts with dynamin and regulates endocytosis by forming vesicotubular structures
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Data indicate that PCH protein family members such as FBP17 couple membrane deformation to actin cytoskeleton reorganization in various cellular processes.
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FBP17 is recruited to clathrin-coated pits in the late stage of endocytosis, indicating its physiological role.
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N-WASP-WIP complex-mediated actin polymerization is activated by phosphatidylserine-containing membranes depending on membrane curvature in the presence of Toca-1 or FBP17 and in the absence of Cdc42 and phosphatidylinositol (4,5)-bisphosphate.
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formin-binding protein 17 (FBP17) recruits WASP, WASP-interacting protein (WIP), and dynamin-2 to the plasma membrane and that this recruitment is necessary for the formation of podosomes and phagocytic cups.
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Rat rapostlin protein has 93% aa identity to human FBP17.
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FNBP1 family proteins (FNBP1 and TRIP10) consist of FCH, FBH and SH3 domains.
