钙调素与 PI4KA 和 FAM126A 的双重相互作用的可视化

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2024-11-07 DOI:10.1016/j.str.2024.10.010

Qingtong Zhou, Xiao Liu, Ming-Wei Wang

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引用次数: 0

摘要

在本期的《Structure》杂志上，Shaw 等人1 结合低温电子显微镜、HDX-MS 和 AlphaFold3 技术，对 PI4KA-TTC7B-FAM126A-calcineurin 复合物进行了可视化研究，并揭示了钙调素与 PI4KA 和 FAM126A 的双重相互作用。这项工作促进了我们对钙调素调控的 PI4KA 活性的理解，并为进一步探索 PI4KA 在质膜中的作用铺平了道路。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Visualizing the dual interaction of calcineurin with PI4KA and FAM126A

In this issue of Structure, Shaw et al.¹ visualize the PI4KA-TTC7B-FAM126A-calcineurin complex by combining cryo-EM, HDX-MS, and AlphaFold3, and reveal a dual interaction of calcineurin with PI4KA and FAM126A. This work promotes our understanding of calcineurin-regulated PI4KA activity and paves the way for further exploration of the roles of PI4KA in the plasma membrane.

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.