We have previously shown that p115, a vesicle docking protein, binds to two proteins (p130 and p400) in detergent extracts of Golgi membranes. p130 was identified as GM130, a Golgi matrix protein, and was shown to act as a membrane receptor for p115. p400 has now been identified as giantin, a Golgi membrane protein with most of its mass projecting into the cytoplasm. Giantin is found on COPI vesicles and pretreatment with antibodies inhibits both the binding of p115 and the docking of these vesicles with Golgi membranes. In contrast, GM130 is depleted from COPI vesicles and inhibition of the GM130 on Golgi membranes, using either antibodies or an NH2-terminal GM130 peptide, inhibits p115 binding and vesicle docking. Together these results suggest that COPI vesicles are docked by giantin on the COPI vesicles and GM130 on Golgi membranes with p115 providing a bridge.
A Role for Giantin in Docking COPI Vesicles to Golgi Membranes
B. Sönnichsen, E. Jämsä, and B. Dirac-Svejstrup were 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, London WC2A, 3PX, UK. Tel.: 0171-269-3561. Fax: 0171-269-3417. E-mail: [email protected]
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.
Birte Sönnichsen, Martin Lowe, Tim Levine, Eija Jämsä, Barbara Dirac-Svejstrup, Graham Warren; A Role for Giantin in Docking COPI Vesicles to Golgi Membranes . J Cell Biol 9 March 1998; 140 (5): 1013–1021. doi: https://doi.org/10.1083/jcb.140.5.1013
Download citation file:
Sign in
Client Account
Sign in via your Institution
Sign in via your InstitutionSuggested Content
Email alerts
Advertisement
Advertisement