p97 and close encounters of every kind: a brief review

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 elu...

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Bibliographic Details
Published inBiochemical Society transactions Vol. 32; no. Pt 5; p. 715
Main Authors Dreveny, I, Pye, V E, Beuron, F, Briggs, L C, Isaacson, R L, Matthews, S J, McKeown, C, Yuan, X, Zhang, X, Freemont, P S
Format Journal Article
LanguageEnglish
Published England 01.11.2004
Subjects
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
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Summary: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.
ISSN:0300-5127
DOI:10.1042/bst0320715