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

Yangzhuang Wang, Ayano Satoh, Graham Warren, Hemmo H. Meyer

Research output: Contribution to journalArticlepeer-review

131 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)973-978
Number of pages6
JournalJournal of Cell Biology
Issue number7
Publication statusPublished - Mar 29 2004
Externally publishedYes


  • Cdc48
  • Deubiquitinating enzyme
  • Membrane fusion
  • Mitosis
  • Ubiquitin

ASJC Scopus subject areas

  • Cell Biology


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