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

85 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

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Membrane Fusion Proteins
Adenosine Triphosphatases
N-Ethylmaleimide-Sensitive Proteins
Qa-SNARE Proteins
SNARE Proteins
Membrane Fusion
Liver
Cytosol
Rats
Fusion reactions
Membranes
p97 ATPase

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. / Meyer, Hemmo H.; Kondo, Hisao; Warren, Graham.

In: FEBS Letters, Vol. 437, No. 3, 23.10.1998, p. 255-257.

Research output: Contribution to journalArticle

Meyer, Hemmo H. ; Kondo, Hisao ; Warren, Graham. / The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. In: FEBS Letters. 1998 ; Vol. 437, No. 3. pp. 255-257.
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