GEP100/BRAG2: activator of ADP-ribosylation factor 6 for regulation of cell adhesion and actin cytoskeleton via E-cadherin and alpha-catenin.

ABSTRACT: GEP(100) (p100) was identified as an ADP-ribosylation factor (ARF) guanine nucleotide-exchange protein (GEP) that partially colocalized with ARF6 in the cell periphery. p100 preferentially accelerated guanosine 5[gamma-thio]triphosphate (GTPgammaS) binding by ARF6, which participates in protein trafficking near the plasma membrane, including receptor recycling, cell adhesion, and cell migration. Here we report that yeast two-hybrid screening of a human fetal brain cDNA library using p100 as bait revealed specific interaction with alpha-catenin, which is known as a regulator of adherens junctions and actin cytoskeleton remodeling. Interaction of p100 with alpha-catenin was confirmed by coimmunoprecipitation of the endogenous proteins from human HepG2 or CaSki cells, although colocalization

SUBMITTER: Hiroi T 

PROVIDER: S-EPMC1502290 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature