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	Biochem. Biophys. Res. Commun. Jun (2003); 306(1):79-86
MICAL-1 isoforms, novel rab1 interacting proteins.
Weide T, Teuber J, Bayer M, Barnekow A
Department of Experimental Tumorbiology, University of Muenster, Badestr. 9, D-48149, Muenster, Germany.
Abstract: Rab1 GTPases participate in regulating the vesicular transport of ER-Golgi compartments. Recently, GM130, p115, and Golgin-84 were identified as effectors of the active conformation of rab1. Here, we describe a novel protein, MICAL-1b, a splice variant of the MICAL-1a protein. Using the yeast two-hybrid system, we showed that it specifically interacts with rab1 in a nucleotide-dependent manner. The interaction was confirmed by GST pulldown experiments. Cell fractionation revealed that in contrast to the mainly membrane-associated rab1 effector GM130, MICAL-1 displays a predominantly cytosolic localization. We mapped the rab1 interacting domain to the C-terminus of MICAL-1, which also mediates binding to the intermediate filament vimentin. Therefore, the interaction of MICAL-1 and rab1 might provide a link between the Golgi apparatus and the intermediate filament cytoskeleton. We suggest that MICAL-1 isoforms with their multidomain structure are novel rab1 interacting proteins that function as scaffold proteins connecting different components in the cell.
[PUBMED: 12788069]