Functional characterization of human ARF-like proteins, ARL4D and its interacted protein α-catenin
Date Issued
2008
Date
2008
Author(s)
Lin, Chin-Tsz
Abstract
ARL4D is a developmentally regulated protein which belongs to ADP-ribosylation factor/ARF-like protein (ARF/ARL) family of Ras-related small G proteins. Recently we demonstrated that ARL4D acts as a novel upstream regulator of a guanine nucleotide-exchange factor (GEF), cytohesin-2/ARNO, to promote ARF6 activation and modulate actin remodeling. Here we show that ARL4D interacts with α-catenin, an essential component of adherens junctions (AJs). The residues 266-657 of α-catenin interact with ARL4D in a GTP-dependent manner. Overexpressing ARL4D and its putative active form, ARL4D(Q80L) caused lateral membranes disorganized in Madin-Darby canine kidney (MDCK) epithelial cells. As a consequence, the AJs structure was defective. The lateral membranes appeared less vertical and had convoluted edges in the cells expressing ARL4D and ARL4D(Q80L), but not ARL4D(T35N), a putative GTP-binding defective mutant. Together, our findings suggest that ARL4D affects the stabilization of α–catenin at the cell cortex and alters the structure of AJs complex.
Subjects
ARF-like proteins
ARL4D
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