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
Department of Biological Sciences, Centre for Structural Biology, Imperial College London, South Kensington, London SW7 2AZ, UK.
Biochem Soc Trans. 2004 Nov;32(Pt 5):715-20. doi: 10.1042/BST0320715.
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.
与多种细胞活动相关的ATP酶(AAA,ATPase associated with various cellular activities),即p97,是一种具有伴侣样功能的六聚体蛋白,据报道它能与许多功能看似不相关的蛋白质相互作用。我们首次报道了这些蛋白质的分类,并旨在阐明它们可能共有的任何共同结构或功能特征。相互作用蛋白被分为两类,一类含有泛素调节X结构域,推测它们与p97的结合方式与p47衔接蛋白相同;另一类是不同功能亚组的非泛素调节X结构域蛋白,它们可能采用不同的相互作用模式(假设它们也直接与p97结合且不是实验假象)。未来的研究将表明相互作用蛋白是将p97导向不同的细胞途径还是共同的途径,而对这些相互作用的结构解析对于理解这些潜在功能至关重要。