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Published online 22 March 2004. doi:10.1083/jcb.200401010
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 164, Number 7, 973-978
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Report

 VCIP135 acts as a deubiquitinating enzyme during p97–p47-mediated reassembly of mitotic Golgi fragments

Yanzhuang Wang2, Ayano Satoh2, Graham Warren2, and Hemmo H. Meyer1

1 Institute of Biochemistry, Swiss Federal Institute of Technology Zurich (ETH), ETH Hoenggerberg, 8093 Zurich, Switzerland
2 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520

Address correspondence to Hemmo H. Meyer, Institute of Biochemistry, ETH Hoenggerberg, HPM G17.1, 8093 Zurich, Switzerland. Tel.: 41-1-633-6634. Fax: 41-1-632-1298. email: hemmo.meyer{at}bc.biol.ethz.ch


Abstract
The AAA-ATPase p97/Cdc48 functions in different cellular pathways using distinct sets of adapters and other cofactors. Together with its adaptor Ufd1–Npl4, it extracts ubiquitylated substrates from the membrane for subsequent delivery to the proteasome during ER-associated degradation. Together with its adaptor p47, on the other hand, it regulates several membrane fusion events, including reassembly of Golgi cisternae after mitosis. The finding of a ubiquitin-binding domain in p47 raises the question as to whether the ubiquitin–proteasome system is also involved in membrane fusion events. Here, we show that p97–p47-mediated reassembly of Golgi cisternae requires ubiquitin, but is not dependent on proteasome-mediated proteolysis. Instead, it requires the deubiquitinating activity of one of its cofactors, VCIP135, which reverses a ubiquitylation event that occurs during mitotic disassembly. Together, these data reveal a cycle of ubiquitylation and deubiquitination that regulates Golgi membrane dynamics during mitosis. Furthermore, they represent the first evidence for a proteasome-independent function of p97/Cdc48.

Key Words: Cdc48; deubiquitinating enzyme; membrane fusion; ubiquitin; mitosis

Abbreviations used in this paper: MGF, mitotic Golgi fragment; MVB, multivesicular body; NSF, N-ethylmaleimide–sensitive factor; SNARE, soluble NSF attachment protein receptor; VCIP135, VCP(p97)/p47 complex–interacting protein of 135 kD.


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