Vps4p底物招募与自抑制释放的底物结合及偶联机制
Substrate binding and coupled mechanisms of Vps4p substrate recruitment and release from autoinhibition.
作者信息
Wienkers Henry, Han Han, Whitby Frank, Hill Christopher P
机构信息
Department of Biochemistry, University of Utah, Salt Lake City, UT, 84112-5650, USA.
出版信息
Sci Rep. 2025 Jul 11;15(1):25024. doi: 10.1038/s41598-025-08418-z.
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 revealed unexpected sequence preference to the substrate binding groove and an elegant mechanism of regulation that couples localization to substrate with release from autoinhibition.
内体分选转运复合体（ESCRT）途径的AAA+型ATP酶Vps4p重塑ESCRT-III复合体以驱动膜裂变。在此，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性以及一种将定位与底物相结合并从自抑制中释放的精妙调控机制。
Zotero 插件