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

FEBS Lett. 1998 Oct 23;437(3):255-7. doi: 10.1016/s0014-5793(98)01232-0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Carrier Proteins / metabolism*
  • Carrier Proteins / physiology*
  • Cytosol / enzymology
  • Enzyme Activation / drug effects
  • Liver / enzymology
  • Membrane Fusion*
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology*
  • Protein Binding
  • Rats
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins*


  • Carrier Proteins
  • Membrane Proteins
  • Nsfl1c protein, rat
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Vesicular Transport Proteins
  • Adenosine Triphosphatases