Vps4 底物结合以及 Vps4p 底物招募和解除自抑制的耦合机制

bioRxiv - Biochemistry Pub Date : 2024-09-07 DOI:10.1101/2024.09.07.611824

Henry Wienkers, Han Han, Frank Whitby, Christopher Hill

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引用次数: 0

摘要

ESCRT通路的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动抑制机制。我们的研究结果揭示了对底物结合槽的意外序列偏好，以及一种将定位到底物与解除自动抑制结合起来的优雅调控机制。

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

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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bioRxiv - Biochemistry

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