Golgin-84 is a rab1 Binding Partner Involved in Golgi Structure

Authors

  • Ayano Satoh,

    1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520–8002. USA
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  • Yanzhuang Wang,

    1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520–8002. USA
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  • Jörg Malsam,

    1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520–8002. USA
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  • Matthew B. Beard,

    1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520–8002. USA
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  • Graham Warren

    1. Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, PO Box 208002, New Haven, Connecticut 06520–8002. USA
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Corresponding author: Graham Warren, graham.warren@yale.edu

Abstract

Members of the golgin family of coiled-coil proteins have been implicated in the tethering of vesicles to Golgi membranes and cisternal membranes to each other. Many also bind to rab GTPases. Golgin-84 is a membrane-anchored golgin that we now show binds preferentially to the GTP form of the rab1 GTPase. It is also present throughout the Golgi stack by immuno-EM. Antibodies to golgin-84 inhibit stacking of cisternal membranes in a cell-free assay for Golgi reassembly, whereas the cytoplasmic domain of golgin-84 stimulates stacking and increases the length of re-assembled stacks. Transient expression of golgin-84 in NRK cells helps prevent the disassembly of the Golgi apparatus normally triggered by treatment with brefeldin A. Together these data suggest that golgin-84 is involved in generating and maintaining the architecture of the Golgi apparatus.

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