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解析波形蛋白组装:连接理论模型与实验方法。

Deciphering vimentin assembly: Bridging theoretical models and experimental approaches.

机构信息

Department of Agricultural Biotechnology, Center for Food and Bioconversions, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Republic of Korea.

Department of Agricultural Biotechnology, Center for Food and Bioconversions, and Research Institute for Agriculture and Life Sciences, CALS, Seoul National University, Seoul 08826, Republic of Korea.

出版信息

Mol Cells. 2024 Jul;47(7):100080. doi: 10.1016/j.mocell.2024.100080. Epub 2024 Jun 11.

DOI:10.1016/j.mocell.2024.100080
PMID:38871297
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11267000/
Abstract

The intricate assembly process of vimentin intermediate filaments (IFs), key components of the eukaryotic cytoskeleton, has yet to be elucidated. In this work, we investigated the transition from soluble tetrameric vimentin units to mature 11-nm tubular filaments, addressing a significant gap in the understanding of IF assembly. Through a combination of theoretical modeling and analysis of experimental data, we propose a novel assembly sequence, emphasizing the role of helical turns and gap filling by soluble tetramers. Our findings shed light on the unique structural dynamics of vimentin and suggest broader implications for the general principles of IF formation.

摘要

中间丝(IFs)的错综复杂的组装过程,是真核细胞骨架的关键组成部分,但其尚未被阐明。在这项工作中,我们研究了从可溶性四聚体中间丝单元到成熟的 11nm 管状纤维的转变,解决了中间丝组装理解中的一个重大空白。通过理论建模和实验数据分析的结合,我们提出了一个新的组装序列,强调了螺旋转弯和可溶性四聚体的间隙填充的作用。我们的发现揭示了中间丝独特的结构动力学,并为中间丝形成的一般原则提供了更广泛的意义。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/51208394f682/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/d5af9ff90002/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/de30b8c3e63b/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/6bf7144b2ab8/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/344dcafdd156/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/51208394f682/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/d5af9ff90002/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/de30b8c3e63b/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/6bf7144b2ab8/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/344dcafdd156/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1bf9/11267000/51208394f682/gr5.jpg

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本文引用的文献

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Nat Struct Mol Biol. 2024 Jun;31(6):939-949. doi: 10.1038/s41594-024-01261-2. Epub 2024 Apr 17.
2
Plasticity of cytoplasmic intermediate filament architecture determines cellular functions.细胞质中间丝结构的可塑性决定了细胞的功能。
Curr Opin Cell Biol. 2023 Dec;85:102270. doi: 10.1016/j.ceb.2023.102270. Epub 2023 Nov 1.
3
Molecular structure of soluble vimentin tetramers.可溶性波形蛋白四聚体的分子结构。
Sci Rep. 2023 May 31;13(1):8841. doi: 10.1038/s41598-023-34814-4.
4
Lamin Filament Assembly Derived from the Atomic Structure of the Antiparallel Four-Helix Bundle.层粘连蛋白丝组装源自于反平行四螺旋束的原子结构。
Mol Cells. 2023 May 31;46(5):309-318. doi: 10.14348/molcells.2023.2144. Epub 2023 May 3.
5
Quo Vadis Experimental Structural Biology?实验结构生物学何去何从?
Mol Cells. 2023 Feb 28;46(2):71-73. doi: 10.14348/molcells.2023.2197.
6
Stability profile of vimentin rod domain.中间纤维丝相关蛋白的稳定性分析。
Protein Sci. 2022 Dec;31(12):e4505. doi: 10.1002/pro.4505.
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