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    A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal

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    Authors
    Corvera, Silvia
    Chawla, Anil
    Chakrabarti, Ranjan
    Joly, Marguerite
    Buxton, Joanne M.
    Czech, Michael P.
    UMass Chan Affiliations
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    1994-08-01
    Keywords
    Amino Acid Sequence
    Animals
    CHO Cells
    Cell Line
    Cercopithecus aethiops
    Coated Pits, Cell-Membrane
    Cricetinae
    Deoxyglucose
    *Endocytosis
    Epitopes
    Glucose Transporter Type 1
    Glucose Transporter Type 4
    Humans
    Kinetics
    *Leucine
    Molecular Sequence Data
    Monosaccharide Transport Proteins
    *Muscle Proteins
    Mutagenesis, Site-Directed
    Rats
    Recombinant Fusion Proteins
    Sequence Homology, Amino Acid
    Transferrin
    Cell Biology
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    Abstract
    The unique COOH-terminal 30-amino acid region of the adipocyte/skeletal muscle glucose transporter (GLUT4) appears to be a major structural determinant of this protein's perinuclear localization, from where it is redistributed to the cell surface in response to insulin. To test whether an underlying mechanism of this domain's function involves glucose transporter endocytosis rates, transfected cells were generated expressing exofacial hemagglutinin epitope (HA)-tagged erythrocyte/brain glucose transporter (GLUT1) or a chimera containing the COOH-terminal 30 amino acids of GLUT4 substituted onto this GLUT1 construct. Incubation of COS-7 or CHO cells expressing the HA-tagged chimera with anti-HA antibody at 37 degrees resulted in an increased rate of antibody internalization compared to cells expressing similar levels of HA-tagged GLUT1, which displays a cell surface disposition. Colocalization of the internalized anti-HA antibody in vesicular structures with internalized transferrin and with total transporters was established by digital imaging microscopy, suggesting the total cellular pool of transporters are continuously recycling through the coated pit endocytosis pathway. Mutation of the unique double leucines 489 and 490 in the rat GLUT4 COOH-terminal domain to alanines caused the HA-tagged chimera to revert to the slow endocytosis rate and steady-state cell surface display characteristic of GLUT1. These results support the hypothesis that the double leucine motif in the GLUT4 COOH terminus operates as a rapid endocytosis and retention signal in the GLUT4 transporter, causing its localization to intracellular compartments in the absence of insulin.
    Source
    J Cell Biol. 1994 Aug;126(4):979-89.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42622
    PubMed ID
    7519625
    Related Resources
    Link to Article in PubMed
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    UMass Chan Faculty and Researcher Publications

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