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First published online September 26, 2003
doi: 10.1242/10.1242/jcs.00817
Commentary |
School of Biological Sciences, University of Manchester, Oxford Road, Manchester M13 9PT, UK
(e-mail: philip.woodman{at}man.ac.uk)
A topic that is keeping cell biologists across several fields occupied is how the AAA ATPase p97 can have so many apparently unrelated functions. A recent model that proposed sets of adaptors for p97 selected according to the type of p97 activity seemed to afford a simple solution. For example, one known adaptor, the Ufd1–Npl4 complex, has been implicated in ubiquitin-dependent proteolysis whereas another, p47, is an essential co-factor for membrane fusion. However, further investigation has revealed that the situation is more complicated. Both Ufd1–Npl4 and p47 adaptors bind ubiquitin, and so their activities may be more closely related than first thought. A role for ubiquitin in p97-dependent membrane fusion is a particularly surprising development with no obvious explanation. However, some clues may be found from looking at the role of ubiquitin and the AAA ATPase Vps4 during sorting on the endocytic pathway.
Key words: AAA ATPase, Cdc48, Proteasome, Ubiquitin, SNARE
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