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 language | English |
|---|---|
| Pages (from-to) | 255-257 |
| Number of pages | 3 |
| Journal | FEBS Letters |
| Volume | 437 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Oct 23 1998 |
| Externally published | Yes |
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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 journal › Article
}
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
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.
UR - http://www.scopus.com/inward/record.url?scp=0032561398&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032561398&partnerID=8YFLogxK
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 -