Decoding the byssus fabrication by spatiotemporal secretome analysis of scallop foot.
Decoding the byssus fabrication by spatiotemporal secretome analysis of scallop foot.
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通过扇贝脚的时空分泌组分析解码足丝的制造
DOI：
10.1016/j.csbj.2022.05.048
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发表时间：
2022
影响因子：
6
通讯作者：
中科院分区：
文献类型：
--
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基于一种新的计算策略，对第一个关于扇贝深海附着的分泌蛋白进行了分析。扇贝深海分泌物组涵盖了几乎所有已知的水生胶粘剂的结构元件和功能域。含EGF样结构域的蛋白、富含Tyr的蛋白和含4C重复序列的蛋白是扇贝足丝的主要成分。提出了一种新的扇贝足丝分泌和粘附的“邻近分泌”模型。分泌组几乎参与了所有的生理、发育和病理过程，但目前对无脊椎动物分泌组的研究还缺乏高效的研究策略。粘附分泌是水生无脊椎动物普遍存在的重要生理过程，其蛋白质组成复杂，粘附机制尚未明确，是分泌组学研究的重要课题。在此，我们提出了一个基于时空转录组的扇贝深海分泌组系统分析的计算管道。共鉴定了186个足丝相关蛋白（BRP），这是第一个被鉴定的扇贝足丝粘附分泌蛋白。扇贝深海分泌物组几乎涵盖了所有已知的水生胶粘剂结构元件和功能域，表明该分泌物组分析方法具有高效性和准确性。我们揭示了扇贝足丝的主要成分（包括EGF样结构域蛋白、Tyr富集蛋白和4C重复序列蛋白）以及主要参与足丝快速组装和粘附的相关修饰酶。BRP的时空表达和共表达网络分析表明，在整个足部区域的扇贝足丝蛋白的同时分泌模式，并揭示了它们在足丝分泌上的不同功能。与先前提出的“根启动的分泌和基于延伸的组装”模型相反，我们的研究结果支持了一种新的“足宽同时分泌和原位组装”的扇贝足丝分泌和粘附模型。扇贝深海分泌组的系统分析为了解水生粘着物分泌过程提供了重要线索，也为研究非模式无脊椎动物分泌组提供了通用框架。
The first secretome about scallop byssal adhesion is profiled based on a new computational strategy. Scallop byssal secretome covered almost all of the known structural elements and functional domains of aquatic adhesives. The EGF-like domain containing proteins, the Tyr-rich proteins and 4C-repeats containing proteins are the main components of scallop byssus. A novel “nearby secretion” model of scallop byssus secretion and adhesion is proposed. Secretome is involved in almost all physiological, developmental, and pathological processes, but to date there is still a lack of highly-efficient research strategy to comprehensively study the secretome of invertebrates. Adhesive secretion is a ubiquitous and essential physiological process in aquatic invertebrates with complicated protein components and unresolved adhesion mechanisms, making it a good subject for secretome profiling studies. Here we proposed a computational pipeline for systematic profiling of byssal secretome based on spatiotemporal transcriptomes of scallop. A total of 186 byssus-related proteins (BRPs) were identified, which represented the first characterized secretome of scallop byssal adhesion. Scallop byssal secretome covered almost all of the known structural elements and functional domains of aquatic adhesives, which suggested this secretome-profiling strategy had both high efficiency and accuracy. We revealed the main components of scallop byssus (including EGF-like domain containing proteins, the Tyr-rich proteins and 4C-repeats containing proteins) and the related modification enzymes primarily contributing to the rapid byssus assembly and adhesion. Spatiotemporal expression and co-expression network analyses of BRPs suggested a simultaneous secretion pattern of scallop byssal proteins across the entire region of foot and revealed their diverse functions on byssus secretion. In contrast to the previously proposed “root-initiated secretion and extension-based assembly” model, our findings supported a novel “foot-wide simultaneous secretion and in situ assembly” model of scallop byssus secretion and adhesion. Systematic analysis of scallop byssal secretome provides important clues for understanding the aquatic adhesive secretion process, as well as a common framework for studying the secretome of non-model invertebrates.
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DOI：
10.1017/s0025315400045616
发表时间：
1979-01-01
影响因子：
1.2
作者：
GRUFFYDD, LD;BUDIMAN, A;NOTT, JA
通讯作者：
NOTT, JA
影响因子：
16
作者：
Hilge, M;Aelen, J;Vuister, GW
通讯作者：
Vuister, GW
扇贝足丝非典型金属蛋白酶抑制剂类蛋白 (Sbp8-1) 的表征
影响因子：
4
作者：
Zhang X;Dai X;Wang L;Miao Y;Xu P;Liang P;Dong B;Bao Z;Wang S;Lyu Q;Liu W
通讯作者：
Liu W
DOI：
10.1107/s0907444909018745
发表时间：
2009-08-01
影响因子：
2.2
作者：
Alonso-Garcia, Noelia;Ingles-Prieto, Alvaro;de Pereda, Jose M.
通讯作者：
de Pereda, Jose M.
DOI：
10.1111/j.2517-6161.1995.tb02031.x
发表时间：
1995-01-01
影响因子：
5.8
作者：
BENJAMINI, Y;HOCHBERG, Y
通讯作者：
HOCHBERG, Y