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Vps4底物结合以及Vps4p底物自抑制募集与释放的偶联机制。

Vps4 substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.

作者信息

Wienkers H J, Han H, Whitby F G, Hill C P

机构信息

Department of Biochemistry, University of Utah, Salt Lake City, Utah, USA.

出版信息

bioRxiv. 2024 Sep 7:2024.09.07.611824. doi: 10.1101/2024.09.07.611824.

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.

摘要

ESCRT途径的AAA+ATP酶Vps4p重塑ESCRT-III复合物以驱动膜裂变。在这里,我们使用肽结合试验来进一步了解底物特异性和自抑制机制。我们的结果揭示了底物结合凹槽出人意料的序列偏好,以及一种将定位与底物偶联并从自抑制中释放的精妙调控机制。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/3572/11398535/608d0e59cef6/nihpp-2024.09.07.611824v1-f0013.jpg

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