p97 and close encounters of every kind: a brief review

Author:

Dreveny I.1,Pye V.E.1,Beuron F.1,Briggs L.C.1,Isaacson R.L.1,Matthews S.J.1,McKeown C.1,Yuan X.1,Zhang X.1,Freemont P.S.1

Affiliation:

1. Department of Biological Sciences, Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, U.K.

Abstract

The AAA (ATPase associated with various cellular activities) ATPase, p97, is a hexameric protein of chaperone-like function, which has been reported to interact with a number of proteins of seemingly unrelated functions. For the first time, we report a classification of these proteins and aim to elucidate any common structural or functional features they may share. The interactors are grouped into those containing ubiquitin regulatory X domains, which presumably bind to p97 in the same way as the p47 adaptor, and into non-ubiquitin regulatory X domain proteins of different functional subgroups that may employ a different mode of interaction (assuming they also bind directly to p97 and are not experimental artifacts). Future studies will show whether interacting proteins direct p97 to different cellular pathways or a common one and structural elucidation of these interactions will be crucial in understanding these underlying functions.

Publisher

Portland Press Ltd.

Subject

Biochemistry

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