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 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.
Dreveny
I
I
Department of Biological Sciences, Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, UK.
Pye
V E
VE
Beuron
F
F
Briggs
L C
LC
Isaacson
R L
RL
Matthews
S J
SJ
McKeown
C
C
Yuan
X
X
Zhang
X
X
Freemont
P S
PS
D000818:Animals; D000951:Antigens, Neoplasm; D018797:Cell Cycle Proteins / Q000737:chemistry; D006801:Humans; D058950:Melanoma-Specific Antigens; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D009363:Neoplasm Proteins / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D025801:Ubiquitin / Q000737:chemistry / Q000378:metabolism
D000951:Antigens, Neoplasm; D018797:Cell Cycle Proteins; D058950:Melanoma-Specific Antigens; D018832:Molecular Chaperones; D009363:Neoplasm Proteins; D025801:Ubiquitin