The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97.
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.
Meyer
H H
HH
Cell Biology Laboratory, Imperial Cancer Research Fund, London, UK.
Kondo
H
H
Warren
G
G
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism* / Q000502:physiology*; D003600:Cytosol / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D008099:Liver / Q000201:enzymology; D008561:Membrane Fusion; D008565:Membrane Proteins / Q000378:metabolism* / Q000502:physiology*; D011485:Protein Binding; D051381:Rats; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D033921:Vesicular Transport Proteins
D002352:Carrier Proteins; D008565:Membrane Proteins; C498751:Nsfl1c protein, rat; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D033921:Vesicular Transport Proteins; D000251:Adenosine Triphosphatases