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The ATPase VCP/p97 functions as a disaggregase against toxic Huntingtin‐exon1 aggregates

Intracellular protein aggregation is characterized by accumulation of misfolded proteins. Chaperones, degradation machineries, and quality‐control mechanisms counteract protein aggregation. In this study, we report that the ATPase valosin‐containing protein (VCP/p97) acts as a functional disaggregase that disassembles Huntingtin‐exon1 aggregates in vitro and in HeLa cells. The N‐terminal part of VCP (Cdc48_N domain) interacts with the N‐terminal 17‐amino acid region of Huntingtin‐exon1. We show that VCP has properties of a disaggregase, since it is capable of reducing preformed protein aggregates and displays increased ATPase activity in the presence of protein aggregates. However, VCP shows high divergence/disparity from other disaggregases. Taken together, our studies show the novel function of VCP/p97 as a disaggregase which detangles protein aggregates to probably channelize their degradation.