PACSIN2 Antibody - #DF12684

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. Also promotes the protrusion engulfment during cell-to-cell spread of bacterial pathogens like Listeria monocytogenes.

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).

Cytoplasm. Cytoplasm>Cytoskeleton. Cytoplasmic vesicle membrane>Peripheral membrane protein>Cytoplasmic side. Early endosome. Recycling endosome membrane. Cell projection>Ruffle membrane>Peripheral membrane protein>Cytoplasmic side. Cell membrane>Peripheral membrane protein>Cytoplasmic side. Cell projection. Membrane>Caveola.
Note: Detected at the neck of flask-shaped caveolae. Localization to tubular recycling endosomes probably requires interaction with MICALL1 and EHD1.

Widely expressed.

Homodimer (By similarity). May form heterooligomers with other PACSINs (By similarity). Interacts (via NPF motifs) with EHD1 (via EH domain). Interacts (via NPF motifs) with EHD2 (via EH domain); this interaction probably stabilizes the caveolae. Interacts with EHD3. Interacts (via the SH3 domain) with MICALL1. Interacts with RAC1. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL (By similarity). Interacts (via F-BAR domain) with CAV1 (By similarity). Interacts with TRPV4 (By similarity).

(Microbial infection) Interacts with ubiquitinated HIV-1 gag (via p6-gag domain); this interaction allows PACSIN2 recruitment to viral assembly sites and its subsequent incorporation into virions.

(Microbial infection) Interacts (via F-BAR domain) with Rous sarcoma virus p2B; this interaction allows PACSIN2 recruitment to viral assembly sites.

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.

Belongs to the PACSIN family.