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形态发生的驱动因素:膜上曲率传感器的自组装

Drivers of Morphogenesis: Curvature Sensor Self-Assembly at the Membrane.

作者信息

Curtis Brandy N, Gladfelter Amy S

机构信息

Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Department of Cell Biology, Duke University, Durham, North Carolina 27708, USA.

出版信息

Cold Spring Harb Perspect Biol. 2024 Dec 2;16(12):a041528. doi: 10.1101/cshperspect.a041528.

DOI:10.1101/cshperspect.a041528
PMID:38697653
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11610757/
Abstract

This review examines the relationships between membrane chemistry, curvature-sensing proteins, and cellular morphogenesis. Curvature-sensing proteins are often orders of magnitude smaller than the membrane curvatures they localize to. How are nanometer-scale proteins used to sense micrometer-scale membrane features? Here, we trace the journey of curvature-sensing proteins as they engage with lipid membranes through a combination of electrostatic and hydrophobic interactions. We discuss how curvature sensing hinges on membrane features like lipid charge, packing, and the directionality of membrane curvature. Once bound to the membrane, many curvature sensors undergo self-assembly (i.e., they oligomerize or form higher-order assemblies that are key for initiating and regulating cell shape transformations). Central to these discussions are the micrometer-scale curvature-sensing proteins' septins. By discussing recent literature surrounding septin membrane association, assembly, and their many functions in morphogenesis with support from other well-studied curvature sensors, we aim to synthesize possible mechanisms underlining cell shape sensing.

摘要

本综述探讨了膜化学、曲率感应蛋白与细胞形态发生之间的关系。曲率感应蛋白的大小通常比它们所定位的膜曲率小几个数量级。纳米级的蛋白质是如何用于感知微米级的膜特征的呢?在这里,我们追踪曲率感应蛋白通过静电和疏水相互作用与脂质膜结合的过程。我们讨论了曲率感应如何取决于膜的特征,如脂质电荷、堆积以及膜曲率的方向性。一旦与膜结合,许多曲率传感器会进行自我组装(即它们会寡聚或形成更高阶的组装体,这对于启动和调节细胞形状转变至关重要)。这些讨论的核心是微米级的曲率感应蛋白——septin。通过讨论围绕septin膜结合、组装及其在形态发生中的多种功能的最新文献,并得到其他经过充分研究的曲率传感器的支持,我们旨在综合出细胞形状感知背后可能的机制。

相似文献

1
Drivers of Morphogenesis: Curvature Sensor Self-Assembly at the Membrane.形态发生的驱动因素:膜上曲率传感器的自组装
Cold Spring Harb Perspect Biol. 2024 Dec 2;16(12):a041528. doi: 10.1101/cshperspect.a041528.
2
Curvature sensing as an emergent property of multiscale assembly of septins.弯曲感应是 septin 多尺度组装的一个新兴特性。
Proc Natl Acad Sci U S A. 2023 Feb 7;120(6):e2208253120. doi: 10.1073/pnas.2208253120. Epub 2023 Jan 30.
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An amphipathic helix enables septins to sense micrometer-scale membrane curvature.一个两亲性螺旋使 septin 能够感知微米级的膜曲率。
J Cell Biol. 2019 Apr 1;218(4):1128-1137. doi: 10.1083/jcb.201807211. Epub 2019 Jan 18.
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Physical limits to membrane curvature sensing by a single protein.单个蛋白对膜曲率感知的物理限制。
Phys Rev E. 2023 Dec;108(6-1):064407. doi: 10.1103/PhysRevE.108.064407.
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Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions.在膜上重组Septin组装以研究生物物理性质和功能。
J Vis Exp. 2022 Jul 28(185). doi: 10.3791/64090.
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Reconstituted in vitro systems to reveal the roles and functions of septins.重建体外系统以揭示septin蛋白的作用和功能。
J Cell Sci. 2023 Oct 1;136(19). doi: 10.1242/jcs.259448. Epub 2023 Oct 10.
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Micron-scale plasma membrane curvature is recognized by the septin cytoskeleton.微米级的质膜曲率可被丝状肌动蛋白细胞骨架识别。
J Cell Biol. 2016 Apr 11;213(1):23-32. doi: 10.1083/jcb.201512029. Epub 2016 Apr 4.
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Bottom-Up In Vitro Methods to Assay the Ultrastructural Organization, Membrane Reshaping, and Curvature Sensitivity Behavior of Septins.从下至上的体外方法来分析 septin 的超微结构组织、膜重塑和曲率敏感性行为。
J Vis Exp. 2022 Aug 17(186). doi: 10.3791/63889.
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Septin assemblies promote the lipid organization of membranes.Septin聚合体促进膜的脂质组织。
Structure. 2025 Mar 6;33(3):451-464.e5. doi: 10.1016/j.str.2025.01.005. Epub 2025 Jan 31.
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Interplay of septin amphipathic helices in sensing membrane-curvature and filament bundling. septin 两性螺旋的相互作用在感知膜曲率和丝束捆绑中。
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引用本文的文献

1
Septin higher-order structure on yeast membranes in vitro.体外酵母细胞膜上的Septin高阶结构。
Nat Commun. 2025 May 30;16(1):5055. doi: 10.1038/s41467-025-60344-w.
2
Rearranging to resist cell death.重新排列以抵抗细胞死亡。
Elife. 2024 Dec 16;13:e104942. doi: 10.7554/eLife.104942.