The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation (PubMed:19549836). Autoinhibition of these functions is mediated by an interaction between the SH3 and F-BAR domains (PubMed:20188097, PubMed:23236520). The F-Bar domain also mediates the binding to the cell actin cytoskeleton through the interaction with CAV-1 (By similarity).
(Microbial infection) The SH3 domain is required for the cell-to-cell spreading of HIV-1 virions.
Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.
(Microbial infection) Specifically enhances the efficiency of HIV-1 virion spread by cell-to-cell transfer (PubMed:29891700). Also promotes the protrusion engulfment during cell-to-cell spread of bacterial pathogens like Listeria monocytogenes (PubMed:31242077). Involved in lipid droplet formation, which is important for HCV virion assembly (PubMed:31801866).
Phosphorylated by casein kinase 2 (CK2). Phosphorylation by PKC probably decreases the membrane binding and tubulation capacities of PACSIN2, thereby modulating the lifetime of caveolae (By similarity).
Belongs to the PACSIN family.
Widely expressed.
Protein kinase C and casein kinase substrate in neurons protein 2, Syndapin-2, Syndapin-II, SdpII, PACSIN2
Proteins
Neuroscience
55739Da
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