The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97

Hemmo H. Meyer, Hisao Kondo, Graham Warren

Research output: Contribution to journalArticle

88 Citations (Scopus)

Abstract

The highly conserved ATPase p97, a member of the AAA-ATPases, is found in a complex with its co-factor p47 in rat liver cytosol. Previously it had been shown that p97-mediated reassembly of Golgi cisternae from mitotic Golgi fragments requires p47 which mediates the binding of p97 to a Golgi t-SNARE (soluble N-ethylmaleimide-sensitive factor attachment factor receptor), syntaxin 5. Here we show that it also suppresses the ATPase activity of p97 by up to 85% in a dose-dependent and saturable manner suggesting that it has other roles in the membrane fusion cycle. Copyright (C) 1998 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)255-257
Number of pages3
JournalFEBS Letters
Volume437
Issue number3
DOIs
Publication statusPublished - Oct 23 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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