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本文引用的文献

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Amphipathic Motifs Regulate N-BAR Protein Endophilin B1 Auto-inhibition and Drive Membrane Remodeling.两亲性模体调节 N-BAR 蛋白内收蛋白 B1 的自动抑制并驱动膜重塑。
Structure. 2021 Jan 7;29(1):61-69.e3. doi: 10.1016/j.str.2020.09.012. Epub 2020 Oct 20.
2
The cryo-EM structure of the SNX-BAR Mvp1 tetramer.SNX-BAR Mvp1 四聚体的冷冻电镜结构。
Nat Commun. 2020 Mar 20;11(1):1506. doi: 10.1038/s41467-020-15110-5.
3
Recognising the signals for endosomal trafficking.识别内体运输的信号。
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Mammalian Retromer Is an Adaptable Scaffold for Cargo Sorting from Endosomes.哺乳动物内体分拣蛋白复合物是一个适用于从内体分拣货物的多功能支架
Structure. 2020 Apr 7;28(4):393-405.e4. doi: 10.1016/j.str.2020.01.009. Epub 2020 Feb 5.
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Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.利用 X 射线、中子和电子进行高分子结构测定: Phenix 的最新进展。
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6
Molecular identification of a BAR domain-containing coat complex for endosomal recycling of transmembrane proteins.内体蛋白跨膜循环的 BAR 结构域包含包被复合物的分子鉴定。
Nat Cell Biol. 2019 Oct;21(10):1219-1233. doi: 10.1038/s41556-019-0393-3. Epub 2019 Oct 1.
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New tools for automated high-resolution cryo-EM structure determination in RELION-3.用于 RELION-3 中自动化高分辨率冷冻电镜结构测定的新工具。
Elife. 2018 Nov 9;7:e42166. doi: 10.7554/eLife.42166.
8
Structure of the membrane-assembled retromer coat determined by cryo-electron tomography.膜组装的逆行内体衣壳结构通过冷冻电子断层扫描确定。
Nature. 2018 Sep;561(7724):561-564. doi: 10.1038/s41586-018-0526-z. Epub 2018 Sep 17.
9
To degrade or not to degrade: mechanisms and significance of endocytic recycling.降解还是不降解:内吞体循环的机制和意义。
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10
The Retromer Complex and Sorting Nexins in Neurodegenerative Diseases.Retromer复合体与分选连接蛋白在神经退行性疾病中的作用
Front Aging Neurosci. 2018 Mar 26;10:79. doi: 10.3389/fnagi.2018.00079. eCollection 2018.

SNX1 介导的膜重塑结构研究

Structural insights into membrane remodeling by SNX1.

机构信息

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.

National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;

出版信息

Proc Natl Acad Sci U S A. 2021 Mar 9;118(10). doi: 10.1073/pnas.2022614118.

DOI:10.1073/pnas.2022614118
PMID:33658379
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7958236/
Abstract

The sorting nexin (SNX) family of proteins deform the membrane to generate transport carriers in endosomal pathways. Here, we elucidate how a prototypic member, SNX1, acts in this process. Performing cryoelectron microscopy, we find that SNX1 assembles into a protein lattice that consists of helical rows of SNX1 dimers wrapped around tubular membranes in a crosslinked fashion. We also visualize the details of this structure, which provides a molecular understanding of how various parts of SNX1 contribute to its ability to deform the membrane. Moreover, we have compared the SNX1 structure with a previously elucidated structure of an endosomal coat complex formed by retromer coupled to a SNX, which reveals how the molecular organization of the SNX in this coat complex is affected by retromer. The comparison also suggests insight into intermediary stages of assembly that results in the formation of the retromer-SNX coat complex on the membrane.

摘要

分选连接蛋白(SNX)家族的蛋白可使细胞膜变形,在胞内体途径中生成运输载体。在此,我们阐明了典型成员 SNX1 在这个过程中的作用。通过冷冻电镜,我们发现 SNX1 组装成一个蛋白晶格,该晶格由 SNX1 二聚体的螺旋排组成,以交联的方式缠绕在管状膜上。我们还观察到了这个结构的细节,这为理解 SNX1 的各个部分如何有助于其膜变形能力提供了分子基础。此外,我们比较了 SNX1 结构与先前阐明的由 retromer 与 SNX 形成的内体包被复合物的结构,揭示了 retromer 如何影响包被复合物中 SNX 的分子组织。这种比较还为形成膜上 retromer-SNX 包被复合物的组装中间阶段提供了一些见解。