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    Cloning, characterization, and expression of a novel GDP dissociation inhibitor isoform from skeletal muscle

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    Authors
    Shisheva, Assia
    Sudhof, Thomas C.
    Czech, Michael P.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    1994-05-01
    Keywords
    Amino Acid Sequence
    Animals
    Base Sequence
    Blotting, Northern
    Brain
    Cell Line
    Cloning, Molecular
    DNA Primers
    GTP-Binding Proteins
    Glutathione Transferase
    *Guanine Nucleotide Dissociation Inhibitors
    Humans
    Liver
    Molecular Sequence Data
    Muscles
    Myocardium
    Organ Specificity
    Pancreas
    Polymerase Chain Reaction
    RNA
    RNA, Messenger
    Rats
    Recombinant Fusion Proteins
    Sequence Homology, Amino Acid
    Sequence Homology, Nucleic Acid
    Species Specificity
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    Cellular mechanisms for controlling membrane trafficking appear to involve small GTP-binding proteins such as the Rab proteins. Rab function is regulated by GDP dissociation inhibitor (GDI), which releases Rab proteins from membranes and inhibits GDP dissociation. Here we report the isolation of a full-length cDNA encoding a novel GDI isoform of 445 amino acids (GDI-2) with a deduced molecular weight of 50,649 from mouse skeletal muscle. Full-length and partial cDNA clones encoding a previously reported GDI protein (GDI-1) were also isolated from cDNA libraries prepared from rat brain and mouse skeletal muscle, respectively. The degree of deduced amino acid sequence identity between mouse GDI-2 and our mouse GDI-1 cDNA clone is 86%. Northern (RNA blot) analysis revealed that in human tissues, both GDI-1 and GDI-2 transcripts were abundant in brain, skeletal muscle, and pancreas but were weakly expressed in heart and liver. GDI-1 mRNA was expressed in kidney, whereas GDI-2 was almost absent, while in lung the relative amounts of these mRNA species were reversed. Specific antibodies against mouse GDI-1 and GDI-2 based on unique peptide sequences in the proteins were raised. Differentiation of 3T3-L1 fibroblasts into highly insulin-responsive adipocytes was accompanied by large increases in both mRNA and protein levels of GDI-1 and GDI-2. GDI-1 and GDI-2 expressed as glutathione S-transferase fusion proteins were both able to solubilize the membrane-bound forms of Rab4 and Rab5 in a GDP/GTP-dependent manner. Taken together, these data demonstrate that the protein products of at least two genes regulate the membrane dynamics of Rab proteins in mice.
    Source
    Mol Cell Biol. 1994 May;14(5):3459-68.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/38596
    PubMed ID
    7513052
    Related Resources
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