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Protein kinase C and casein kinase substrate in neurons protein 2

Domain

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.

Function

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).

Post-translational modifications

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).

Sequence Similarities

Belongs to the PACSIN family.

Tissue Specificity

Widely expressed.

Cellular localization

Alternative names

Protein kinase C and casein kinase substrate in neurons protein 2, Syndapin-2, Syndapin-II, SdpII, PACSIN2

swissprot:Q9UNF0 omim:604960 entrezGene:11252