MICAL-1 isoforms, novel rab1 interacting proteins.

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.
Mesh Terms:
Animals, Binding Sites, Biological Transport, Active, Cell Line, Cricetinae, Cytoskeletal Proteins, Cytosol, Endoplasmic Reticulum, Golgi Apparatus, Guanosine Triphosphate, Humans, Intracellular Signaling Peptides and Proteins, Protein Binding, Protein Isoforms, Protein Structure, Tertiary, Sequence Deletion, Two-Hybrid System Techniques, Vimentin, rab1 GTP-Binding Proteins
Biochem. Biophys. Res. Commun.
Date: Jun. 20, 2003
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