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The p47 co‐factor regulates the ATPase activity of the membrane fusion protein, p97
Author(s) -
Meyer Hemmo H,
Kondo Hisao,
Warren Graham
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01232-0
Subject(s) - chemistry , lipid bilayer fusion , atpase , fusion , fusion protein , microbiology and biotechnology , membrane , biochemistry , biophysics , biology , enzyme , recombinant dna , philosophy , gene , linguistics
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.