Ghosh, D.K. and Roy, Ajit and Ranjan, Akash (2018) The ATPase VCP/p97 functions as a disaggregase against toxic Huntingtin-exon1 aggregates. FEBS Letters, 592 (16). pp. 2680-2692. ISSN 0014-5793

Text FEBS Lett 592 p2680.pdf Restricted to Repository staff only Download (1152Kb) | Request a copy

Abstract

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

Item Type:	Article
Uncontrolled Keywords:	Huntingtin-exon1 aggregates, VCP/p97, Disaggregase
Depositing User:	Users 2 not found.
Date Deposited:	11 Aug 2018 10:49
Last Modified:	08 Sep 2018 11:36
URI:	http://cdfd.sciencecentral.in/id/eprint/858

Actions (login required)

View Item