前蛋白转化酶BLI-4在秀丽隐杆线虫角质层组装之前促进胶原蛋白分泌。

IF 4.5 2区 生物学 Q1 Agricultural and Biological Sciences
PLoS Genetics Pub Date : 2023-09-18 eCollection Date: 2023-09-01 DOI:10.1371/journal.pgen.1010944
Susanna K Birnbaum, Jennifer D Cohen, Alexandra Belfi, John I Murray, Jennifer R G Adams, Andrew D Chisholm, Meera V Sundaram
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引用次数: 0

摘要

一些类型的胶原蛋白,包括跨膜MACIT胶原蛋白和秀丽隐杆线虫角质层胶原蛋白,在一个类似于弗林蛋白酶或枯草杆菌蛋白酶/可辛(PCSK)家族的其他前蛋白转化酶的共有位点上被N-末端切割。这种切割可以从质膜释放跨膜胶原,并影响细胞外基质的组装或结构。然而,这种切割的功能后果尚不清楚,也缺乏特定PCSK作用的证据。在这里,我们使用内源性胶原融合荧光蛋白来观察秀丽隐杆线虫中第一个基于胶原的角质层的分泌和组装,然后测试PCSK BLI-4在这些过程中的作用。出乎意料的是,我们发现角质层胶原SQT-3和DPY-17在角质层基质组装前几个小时分泌到胚胎外空间。此外,这种早期分泌依赖于BLI-4/PCSK;在bli-4和切割位点突变体中,SQT-3和DPY-17不能有效分泌,而是形成大的细胞内点状。它们后来组装成角质层基质的过程减少了,但并没有完全阻断。这些数据揭示了胶原N末端处理在细胞内运输和体内基质组装控制中的作用。我们的观察结果还促使对秀丽隐杆线虫角质层基质组装和角质层前到角质层过渡的经典模型进行了修订,表明角质层组装是通过一系列调节步骤进行的,而不仅仅是通过顺序分泌和沉积。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

The proprotein convertase BLI-4 promotes collagen secretion prior to assembly of the Caenorhabditis elegans cuticle.

The proprotein convertase BLI-4 promotes collagen secretion prior to assembly of the Caenorhabditis elegans cuticle.

The proprotein convertase BLI-4 promotes collagen secretion prior to assembly of the Caenorhabditis elegans cuticle.

The proprotein convertase BLI-4 promotes collagen secretion prior to assembly of the Caenorhabditis elegans cuticle.

Some types of collagens, including transmembrane MACIT collagens and C. elegans cuticle collagens, are N-terminally cleaved at a dibasic site that resembles the consensus for furin or other proprotein convertases of the subtilisin/kexin (PCSK) family. Such cleavage may release transmembrane collagens from the plasma membrane and affect extracellular matrix assembly or structure. However, the functional consequences of such cleavage are unclear and evidence for the role of specific PCSKs is lacking. Here, we used endogenous collagen fusions to fluorescent proteins to visualize the secretion and assembly of the first collagen-based cuticle in C. elegans and then tested the role of the PCSK BLI-4 in these processes. Unexpectedly, we found that cuticle collagens SQT-3 and DPY-17 are secreted into the extraembryonic space several hours before cuticle matrix assembly. Furthermore, this early secretion depends on BLI-4/PCSK; in bli-4 and cleavage-site mutants, SQT-3 and DPY-17 are not efficiently secreted and instead form large intracellular puncta. Their later assembly into cuticle matrix is reduced but not entirely blocked. These data reveal a role for collagen N-terminal processing in intracellular trafficking and the control of matrix assembly in vivo. Our observations also prompt a revision of the classic model for C. elegans cuticle matrix assembly and the pre-cuticle-to-cuticle transition, suggesting that cuticle layer assembly proceeds via a series of regulated steps and not simply by sequential secretion and deposition.

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来源期刊
PLoS Genetics
PLoS Genetics 生物-遗传学
CiteScore
8.10
自引率
2.20%
发文量
438
审稿时长
1 months
期刊介绍: PLOS Genetics is run by an international Editorial Board, headed by the Editors-in-Chief, Greg Barsh (HudsonAlpha Institute of Biotechnology, and Stanford University School of Medicine) and Greg Copenhaver (The University of North Carolina at Chapel Hill). Articles published in PLOS Genetics are archived in PubMed Central and cited in PubMed.
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