p97 and close encounters of every kind: A brief review

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

72 Citations (Scopus)

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 jn 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.

Original languageEnglish
Pages (from-to)715-720
Number of pages6
JournalBiochemical Society Transactions
Volume32
Issue number5
DOIs
Publication statusPublished - Nov 2004

Keywords

  • Adaptor
  • Cdc48
  • Interactions
  • P97
  • Valosin-containing protein (VCP)

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