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探索多通道跨膜转运蛋白在其天然膜环境中的分子组成。

Exploring the molecular composition of the multipass translocon in its native membrane environment.

机构信息

https://ror.org/04pp8hn57 Structural Biochemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands.

https://ror.org/04pp8hn57 Structural Biochemistry, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, Netherlands

出版信息

Life Sci Alliance. 2024 Jun 12;7(8). doi: 10.26508/lsa.202302496. Print 2024 Aug.

DOI:10.26508/lsa.202302496
PMID:38866426
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11169918/
Abstract

Multispanning membrane proteins are inserted into the endoplasmic reticulum membrane by the ribosome-bound multipass translocon (MPT) machinery. Based on cryo-electron tomography and extensive subtomogram analysis, we reveal the composition and arrangement of ribosome-bound MPT components in their native membrane environment. The intramembrane chaperone complex PAT and the translocon-associated protein (TRAP) complex associate substoichiometrically with the MPT in a translation-dependent manner. Although PAT is preferentially part of MPTs bound to translating ribosomes, the abundance of TRAP is highest in MPTs associated with non-translating ribosomes. The subtomogram average of the TRAP-containing MPT reveals intermolecular contacts between the luminal domains of TRAP and an unknown subunit of the back-of-Sec61 complex. AlphaFold modeling suggests this protein is nodal modulator, bridging the luminal domains of nicalin and TRAPα. Collectively, our results visualize the variability of MPT factors in the native membrane environment dependent on the translational activity of the bound ribosome.

摘要

多跨膜蛋白由核糖体结合的多通道转位器（MPT）机制插入内质网膜中。基于冷冻电子断层扫描和广泛的亚断层分析，我们揭示了核糖体结合的 MPT 成分在其天然膜环境中的组成和排列。膜内伴侣复合物 PAT 和转位器相关蛋白（TRAP）复合物以翻译依赖性的方式与 MPT 亚化学计量缔合。尽管 PAT 优先成为与翻译核糖体结合的 MPT 的一部分，但 TRAP 的丰度在与非翻译核糖体相关的 MPT 中最高。含有 TRAP 的 MPT 的亚断层平均显示了 TRAP 的腔域与 Sec61 复合体背面的未知亚基之间的分子间接触。AlphaFold 建模表明该蛋白是节点调节剂，连接 nicalin 和 TRAPα 的腔域。总的来说，我们的结果可视化了在结合核糖体的翻译活性依赖性的天然膜环境中 MPT 因子的可变性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/ba10d4938ed6/LSA-2023-02496_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/a0e457999a83/LSA-2023-02496_FigS1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/17ad54282bab/LSA-2023-02496_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/b75390c19ffc/LSA-2023-02496_FigS2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/c611a0d28448/LSA-2023-02496_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/c0992bbb06c6/LSA-2023-02496_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/67cf524eaf38/LSA-2023-02496_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/f0f8b7eecec6/LSA-2023-02496_FigS3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/2e2be13b6a1d/LSA-2023-02496_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/2fad817265c2/LSA-2023-02496_FigS4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/ba10d4938ed6/LSA-2023-02496_Fig6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/a0e457999a83/LSA-2023-02496_FigS1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/17ad54282bab/LSA-2023-02496_Fig1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/b75390c19ffc/LSA-2023-02496_FigS2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/c611a0d28448/LSA-2023-02496_Fig2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/c0992bbb06c6/LSA-2023-02496_Fig3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/67cf524eaf38/LSA-2023-02496_Fig4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/f0f8b7eecec6/LSA-2023-02496_FigS3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/2e2be13b6a1d/LSA-2023-02496_Fig5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/2fad817265c2/LSA-2023-02496_FigS4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/62c6/11169918/ba10d4938ed6/LSA-2023-02496_Fig6.jpg

相似文献

[1]
Exploring the molecular composition of the multipass translocon in its native membrane environment.

Life Sci Alliance. 2024-8

[2]
An ER translocon for multi-pass membrane protein biogenesis.

Elife. 2020-8-21

[3]
Mechanism of an intramembrane chaperone for multipass membrane proteins.

Nature. 2022-11

[4]
Substrate-driven assembly of a translocon for multipass membrane proteins.

Nature. 2022-11

[5]
Structural analysis of the dynamic ribosome-translocon complex.

Elife. 2024-6-18

[6]
Functions and Mechanisms of the Human Ribosome-Translocon Complex.

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[7]
Visualization of translation and protein biogenesis at the ER membrane.

Nature. 2023-2

[8]
Heterogeneous translational landscape of the endoplasmic reticulum revealed by ribosome proximity labeling and transcriptome analysis.

J Biol Chem. 2019-4-19

[9]
Organization of the native ribosome-translocon complex at the mammalian endoplasmic reticulum membrane.

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[10]
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引用本文的文献

[1]
Nodal modulator (NOMO) is a force-bearing transmembrane protein required for muscle differentiation.

J Cell Biol. 2025-9-1

[2]
Structural analysis of the dynamic ribosome-translocon complex.

Elife. 2024-6-18

本文引用的文献

[1]
Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.

EMBO Rep. 2023-12-6

[2]
Molecular basis of the TRAP complex function in ER protein biogenesis.

Nat Struct Mol Biol. 2023-6

[3]
Visualization of translation and protein biogenesis at the ER membrane.

Nature. 2023-2

[4]
Mechanism of an intramembrane chaperone for multipass membrane proteins.

Nature. 2022-11

[5]
Substrate-driven assembly of a translocon for multipass membrane proteins.

Nature. 2022-11

[6]
ColabFold: making protein folding accessible to all.

Nat Methods. 2022-6

[7]
A unified evolutionary origin for the ubiquitous protein transporters SecY and YidC.

BMC Biol. 2021-12-15

[8]
AlphaFold Protein Structure Database: massively expanding the structural coverage of protein-sequence space with high-accuracy models.

Nucleic Acids Res. 2022-1-7

[9]
Take Me Home, Protein Roads: Structural Insights into Signal Peptide Interactions during ER Translocation.

Int J Mol Sci. 2021-11-1

[10]
The mechanisms of integral membrane protein biogenesis.

Nat Rev Mol Cell Biol. 2022-2

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