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.
p97 and close encounters of every kind: a brief review
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I. Dreveny, V.E. Pye, F. Beuron, L.C. Briggs, R.L. Isaacson, S.J. Matthews, C. McKeown, X. Yuan, X. Zhang, P.S. Freemont; p97 and close encounters of every kind: a brief review. Biochem Soc Trans 1 November 2004; 32 (5): 715–720. doi: https://doi.org/10.1042/BST0320715
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