A Role for Giantin in Docking COPI Vesicles to Golgi Membranes

doi:10.1083/jcb.140.5.1013

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© The Rockefeller University Press, 0021-9525/1998//1013 $5.00
The Journal of Cell Biology, Volume 140, Number 5, , 1998 1013-1021

Article

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. Giantinis found on COPI vesicles and pretreatment with antibodies inhibitsboth the binding of p115 and the docking of these vesicleswith Golgi membranes. In contrast, GM130 is depleted from COPIvesicles and inhibition of the GM130 on Golgi membranes, usingeither antibodies or an NH₂-terminal GM130 peptide, inhibitsp115 binding and vesicle docking. Together these results suggestthat COPI vesicles are docked by giantin on the COPI vesiclesand GM130 on Golgi membranes with p115 providing a bridge.

Abbreviations used in this paper: COP, coat protein; DTSSP, 3,3'-dithiobis(sulfosuccinimidyl-propionate); NSF, N-ethylmaleimide–sensitive fusion protein; SNAP, soluble NSF attachment protein; SNARE, SNAP receptor.

B. Sönnichsen, E. Jämsä, and B. Dirac-Svejstrupwere supported by research fellowships from the Deutsche Forschungsgemeinschaft,Academy of Finland, and Danish Natural Science Research Council,respectively.

Address all correspondence to Graham Warren, Cell Biology Laboratory, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, LondonWC2A, 3PX, UK. Tel.: 0171-269-3561. Fax: 0171-269-3417. E-mail:g.warren{at}europa.lif.icnet.uk

B. Sönnichsen's present address is Cell Biology Program,European Molecular Biology Laboratories, Meyerhofstrasse 1,69117 Heidelberg, Germany.

T. Levine's present address is Medical Research Council LMB,Hills Road, Cambridge CB2 2QH, UK.

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