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MICAL-1 isoforms, novel rab1 interacting proteins.

Thomas Weide·Julia Teuber·Michael Bayer·Angelika Barnekow
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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.

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Adaptor Proteins, Signal TransducingAnimalsBinding SitesBiological Transport, ActiveCell LineCricetinaeCytoskeletal ProteinsCytosolEndoplasmic ReticulumGolgi ApparatusGuanosine TriphosphateHumansIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsMicrofilament ProteinsMixed Function OxygenasesProtein BindingProtein IsoformsProtein Structure, TertiarySequence DeletionTwo-Hybrid System TechniquesVimentinrab1 GTP-Binding ProteinsCalponinsJournal ArticleResearch Support, Non-U.S. Gov't

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Thomas Weide, Julia Teuber, Michael Bayer, Angelika Barnekow. 2003-06-20. MICAL-1 isoforms, novel rab1 interacting proteins.. https://doi.org/10.1016/s0006-291x(03)00918-5

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