p97 and close encounters of every kind: a brief review

Biochem Soc Trans. 2004 Nov;32(Pt 5):715-20. doi: 10.1042/BST0320715.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antigens, Neoplasm
  • Cell Cycle Proteins / chemistry
  • Humans
  • Melanoma-Specific Antigens
  • Models, Molecular
  • Molecular Chaperones / metabolism
  • Neoplasm Proteins / metabolism
  • Neoplasm Proteins / physiology*
  • Protein Binding
  • Protein Structure, Tertiary
  • Ubiquitin / chemistry
  • Ubiquitin / metabolism

Substances

  • Antigens, Neoplasm
  • Cell Cycle Proteins
  • Melanoma-Specific Antigens
  • Molecular Chaperones
  • Neoplasm Proteins
  • Ubiquitin