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. Arfaptin 1 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. Arfaptin 1 binds to nonmyristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to ARF1, 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
Uniprot	NM_001025593 Human NP_001020766 Human NP_001020766.1 Human NP_055262 Human NP_055262.1 Human P53367 Human
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