ARFIP1 Products

Description

ADP-ribosylation factors, or ARFs, enhance the ADP ribosyltransferase activity of cholera toxin and are implicated in vesicle transport between endoplasmic reticulum and the Golgi complex. ARFIP1 is recruited from the cytosol to Golgi membranes by ARFs in a guanosine 5'-O-(3-thiotriphosphate)-dependent and brefeldin A-sensitive manner but is not a constituent of coatomer. ARFIP1 binds to nonmyristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to ARFIP1, another class I ARF. It binds with lower affinity to ARF5, a class II ARF, and with very little affinity to ARF6, a class III ARF. POR1 (also designated arfaptin 2) was first isolated as a Rac 1 binding protein necessary for Rac mediated Actin polymerization and the subsequent formation of membrane ruffles and lamellipodia. POR1 has also been shown to interact with the ADP ribosylation factor ARF6, a GTPase that associates with the plasma membrane and intracellular endosome vesicles, in a GTP dependent manner. The association of POR1 with ARF6 stimulates induction of Actin polymerization. POR1 appears to play a regulatory role through multiple signaling pathways in the reorganization of the cytoskeletal structure.

Bioinformatics

Entrez	27236 Human 60382 Rat
Product By Gene ID	27236
Alternate Names	ADP-ribosylation factor interacting protein 1 ADP-ribosylation factor-interacting protein 1 arfaptin 1 arfaptin-1 HSU52521 MGC117369