Journal
FEBS LETTERS
Volume 520, Issue 1-3, Pages 107-110Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02777-1
Keywords
Cdc48; p97; VCP; ATPase associated with various cellular activities; chaperone; ubiquitin; ER-associated protein; Hsp70
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The ATPase Cdc48 is required for membrane fusion and protein degradation. Recently it has been suggested that Cdc48 in a complex with Ufd1 and Np14 acts as an ubiquitin-dependent chaperone. Here it is shown that recombinant Cdc48 alone can distinguish between the native and the non-native conformation of model substrates. First, Cdc48 prevents luciferase from aggregating following a heat shock. Second, it inhibits the aggregation of rhodanese upon dilution. Third, Cdc48 binds specifically to heat-denatured luciferase. These chaperone-like functions seem to be independent of ATPase activity. Furthermore, Cdc48 can act as a co-chaperone in the Hsc70-Hsp40 chaperone system. These results show that Cdc48 possesses chaperone-like activities and can functionally interact with Hsc70. Cdc48's ability to recognise denatured proteins can also be a source of unspecific binding in biochemical interaction experiments. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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