Abstract
Human p97/VCP, an AAA+ ATPase, regulates various cellular activities by interacting with cofactor proteins, including ubiquitin-dependent protein quality control, Golgi-biogenesis, and endoplasmic reticulum-associated degradation (ERAD). Single amino-acid mutation of R155H on the N-domain is the most prevalent, leading to a rare degenerative disease MSP1. The p97 R155H mutant exhibits abnormal ATPase activity and cofactor dysregulation. We pursued biochemical characterization in combination with single-particle cryo-electron microscopy (cryo-EM) to study the interaction of p97R155H mutant with its cofactor p47 and determined the structures of the p97R155H-p47 complex in full length for the first time.
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