TY - JOUR
T1 - The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
AU - Meyer, Hemmo H.
AU - Kondo, Hisao
AU - Warren, Graham
N1 - Funding Information:
This work was supported by a postdoctoral fellowship from the Deutsche Forschungsgemeinschaft to H.H. Meyer.
PY - 1998/10/23
Y1 - 1998/10/23
N2 - 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.
AB - 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.
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U2 - 10.1016/S0014-5793(98)01232-0
DO - 10.1016/S0014-5793(98)01232-0
M3 - Article
C2 - 9824302
AN - SCOPUS:0032561398
VL - 437
SP - 255
EP - 257
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 3
ER -