胶原蛋白 X 从 ER 到高尔基体运输的可视化。

IF 2 4区 生物学 Q4 CELL BIOLOGY
Cell structure and function Pub Date : 2024-10-02 Epub Date: 2024-09-06 DOI:10.1247/csf.24024
Yuan Ximin, Hitoshi Hashimoto, Ikuo Wada, Nobuko Hosokawa
{"title":"胶原蛋白 X 从 ER 到高尔基体运输的可视化。","authors":"Yuan Ximin, Hitoshi Hashimoto, Ikuo Wada, Nobuko Hosokawa","doi":"10.1247/csf.24024","DOIUrl":null,"url":null,"abstract":"<p><p>Collagen is the most abundant protein in the extracellular matrix of animals, and 28 types of collagen have been reported in humans. We previously analyzed the endoplasmic reticulum (ER)-to-Golgi transport of fibril-forming type III collagen (Hirata et al., 2022) and network-forming type IV collagen (Matsui et al., 2020), both of which have long collagenous triple-helical regions. To understand the ER-to-Golgi trafficking of various types of collagens, we analyzed the transport of short-chain type X collagen in this study. We fused cysteine-free GFP to the N-telopeptide region of procollagen X (GFP-COL10A1), as employed in our previous analysis of procollagens III and IV, and analyzed its transport by live-cell imaging. Procollagen X was transported to the Golgi apparatus via vesicular and tubular carriers containing ERGIC53 and RAB1B, similar to those used for procollagen III. Carriers containing procollagen X probably used the same transport processes as those containing conventional cargoes such as α<sub>1</sub>-antitrypsin. SAR1, TANGO1, SLY1/SCFD1, and BET3/TRAPPC3 were required for trafficking of procollagen X, which are different from the factors required for trafficking of procollagens III (SAR1, TANGO1, and CUL3) and IV (SAR1 and SLY1/SCFD1). These findings reveal that accommodation of various types of collagens with different shapes into carriers may require fine-tuning of the ER-to-Golgi transport machinery.Key words: collagen, GFP-procollagen X, ER-to-Golgi trafficking, export from ER, TANGO1.</p>","PeriodicalId":9927,"journal":{"name":"Cell structure and function","volume":" ","pages":"67-81"},"PeriodicalIF":2.0000,"publicationDate":"2024-10-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Visualization of ER-to-Golgi trafficking of procollagen X.\",\"authors\":\"Yuan Ximin, Hitoshi Hashimoto, Ikuo Wada, Nobuko Hosokawa\",\"doi\":\"10.1247/csf.24024\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Collagen is the most abundant protein in the extracellular matrix of animals, and 28 types of collagen have been reported in humans. We previously analyzed the endoplasmic reticulum (ER)-to-Golgi transport of fibril-forming type III collagen (Hirata et al., 2022) and network-forming type IV collagen (Matsui et al., 2020), both of which have long collagenous triple-helical regions. To understand the ER-to-Golgi trafficking of various types of collagens, we analyzed the transport of short-chain type X collagen in this study. We fused cysteine-free GFP to the N-telopeptide region of procollagen X (GFP-COL10A1), as employed in our previous analysis of procollagens III and IV, and analyzed its transport by live-cell imaging. Procollagen X was transported to the Golgi apparatus via vesicular and tubular carriers containing ERGIC53 and RAB1B, similar to those used for procollagen III. Carriers containing procollagen X probably used the same transport processes as those containing conventional cargoes such as α<sub>1</sub>-antitrypsin. SAR1, TANGO1, SLY1/SCFD1, and BET3/TRAPPC3 were required for trafficking of procollagen X, which are different from the factors required for trafficking of procollagens III (SAR1, TANGO1, and CUL3) and IV (SAR1 and SLY1/SCFD1). These findings reveal that accommodation of various types of collagens with different shapes into carriers may require fine-tuning of the ER-to-Golgi transport machinery.Key words: collagen, GFP-procollagen X, ER-to-Golgi trafficking, export from ER, TANGO1.</p>\",\"PeriodicalId\":9927,\"journal\":{\"name\":\"Cell structure and function\",\"volume\":\" \",\"pages\":\"67-81\"},\"PeriodicalIF\":2.0000,\"publicationDate\":\"2024-10-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Cell structure and function\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1247/csf.24024\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/9/6 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q4\",\"JCRName\":\"CELL BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Cell structure and function","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1247/csf.24024","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/9/6 0:00:00","PubModel":"Epub","JCR":"Q4","JCRName":"CELL BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

胶原蛋白是动物细胞外基质中最丰富的蛋白质,据报道人类有 28 种胶原蛋白。我们之前分析了纤维形成的 III 型胶原蛋白(Hirata 等人,2022 年)和网络形成的 IV 型胶原蛋白(Matsui 等人,2020 年)从内质网(ER)到高尔基体的转运,这两种胶原蛋白都具有长胶原三螺旋区域。为了了解各种类型胶原从ER到高尔基体的转运,我们在本研究中分析了短链X型胶原的转运。我们将无半胱氨酸的 GFP 与原胶原 X 的 N-telopeptide 区域(GFP-COL10A1)融合,就像之前分析原胶原 III 和 IV 时所采用的方法一样,并通过活细胞成像分析其运输。原胶原 X 是通过含有 ERGIC53 和 RAB1B 的囊泡和管状载体运输到高尔基体的,这与原胶原 III 使用的载体类似。含有胶原蛋白 X 的载体可能与含有传统货物(如抗胰蛋白酶)的载体使用相同的运输过程。促胶原 X 的运输需要 SAR1、TANGO1、SLY1/SCFD1 和 BET3/TRAPPC3,它们与促胶原 III(SAR1、TANGO1 和 CUL3)和 IV(SAR1 和 SLY1/SCFD1)的运输所需的因子不同。这些发现揭示了将不同形状的各类胶原容纳到载体中可能需要对ER到高尔基体的转运机制进行微调。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Visualization of ER-to-Golgi trafficking of procollagen X.

Collagen is the most abundant protein in the extracellular matrix of animals, and 28 types of collagen have been reported in humans. We previously analyzed the endoplasmic reticulum (ER)-to-Golgi transport of fibril-forming type III collagen (Hirata et al., 2022) and network-forming type IV collagen (Matsui et al., 2020), both of which have long collagenous triple-helical regions. To understand the ER-to-Golgi trafficking of various types of collagens, we analyzed the transport of short-chain type X collagen in this study. We fused cysteine-free GFP to the N-telopeptide region of procollagen X (GFP-COL10A1), as employed in our previous analysis of procollagens III and IV, and analyzed its transport by live-cell imaging. Procollagen X was transported to the Golgi apparatus via vesicular and tubular carriers containing ERGIC53 and RAB1B, similar to those used for procollagen III. Carriers containing procollagen X probably used the same transport processes as those containing conventional cargoes such as α1-antitrypsin. SAR1, TANGO1, SLY1/SCFD1, and BET3/TRAPPC3 were required for trafficking of procollagen X, which are different from the factors required for trafficking of procollagens III (SAR1, TANGO1, and CUL3) and IV (SAR1 and SLY1/SCFD1). These findings reveal that accommodation of various types of collagens with different shapes into carriers may require fine-tuning of the ER-to-Golgi transport machinery.Key words: collagen, GFP-procollagen X, ER-to-Golgi trafficking, export from ER, TANGO1.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Cell structure and function
Cell structure and function 生物-细胞生物学
CiteScore
2.50
自引率
0.00%
发文量
6
审稿时长
>12 weeks
期刊介绍: Cell Structure and Function is a fully peer-reviewed, fully Open Access journal. As the official English-language journal of the Japan Society for Cell Biology, it is published continuously online and biannually in print. Cell Structure and Function publishes important, original contributions in all areas of molecular and cell biology. The journal welcomes the submission of manuscripts on research areas such as the cell nucleus, chromosomes, and gene expression; the cytoskeleton and cell motility; cell adhesion and the extracellular matrix; cell growth, differentiation and death; signal transduction; the protein life cycle; membrane traffic; and organelles.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信