A Role for Giantin in Docking COPI Vesicles to Golgi Membranes

doi:10.1083/jcb.140.5.1013

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J. Cell Biol., Volume 140, Number 5, March 9, 1998 1013-1021

A Role for Giantin in Docking COPI Vesicles to Golgi Membranes

Birte Sönnichsen, Martin Lowe, Tim Levine, Eija Jämsä, Barbara Dirac-Svejstrup, and Graham Warren

Cell Biology Laboratory, Imperial Cancer Research Fund, London WC2A, 3PX, United Kingdom

We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extractsof Golgi membranes. p130 was identified as GM130, a Golgi matrixprotein, and was shown to act as a membrane receptor for p115.p400 has now been identified as giantin, a Golgi membrane proteinwith most of its mass projecting into the cytoplasm. Giantin isfound on COPI vesicles and pretreatment with antibodies inhibitsboth the binding of p115 and the docking of these vesicles withGolgi membranes. In contrast, GM130 is depleted from COPI vesiclesand inhibition of the GM130 on Golgi membranes, using either antibodiesor an NH₂-terminal GM130 peptide, inhibits p115 binding and vesicledocking. Together these results suggest that COPI vesicles aredocked by giantin on the COPI vesicles and GM130 on Golgi membraneswith p115 providing a bridge.

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