
==== Front
bioRxiv
BIORXIV
bioRxiv
2692-8205
Cold Spring Harbor Laboratory

10.1101/2024.09.07.611824
preprint
1
Article
Vps4 substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition
Wienkers HJ http://orcid.org/0000-0001-7948-3241

Han H http://orcid.org/0000-0003-0361-4254

Whitby FG http://orcid.org/0000-0003-3511-2216

Hill CP http://orcid.org/0000-0001-6796-7740

07 9 2024
2024.09.07.611824https://creativecommons.org/licenses/by-nc-nd/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which allows reusers to copy and distribute the material in any medium or format in unadapted form only, for noncommercial purposes only, and only so long as attribution is given to the creator.
http://biorxiv.org/lookup/doi/10.1101/2024.09.07.611824
nihpp-2024.09.07.611824.pdf
Abstract

The ESCRT pathway’s AAA+ ATPase, Vps4p, remodels ESCRT-III complexes to drive membrane fission. Here, we use peptide binding assays to further the understanding of substrate specificity and the mechanism of autoinhibition. Our results reveal unexpected sequence preference to the substrate binding groove and an elegant mechanism of regulation that couples localization to substrate with release from autoinhibition.
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pmc
