Evolution and Diversity of Semaphorins and Plexins in Choanoflagellates.

Evolution and Diversity of Semaphorins and Plexins in Choanoflagellates.
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领鞭毛虫中脑信号蛋白和丛蛋白的进化和多样性。

DOI:
10.1093/gbe/evab035
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发表时间:
2021-03-01
影响因子:
3.3
通讯作者:
Friedel RH
Friedel RH
中科院分区:
生物学2区
文献类型:
--
作者:
Junqueira Alves C;Silva Ladeira J;Hannah T;Pedroso Dias RJ;Zabala Capriles PV;Yotoko K;Zou H;Friedel RH

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信号蛋白和丛蛋白是影响后生动物细胞中细胞骨架动力学的细胞表面配体/受体蛋白。有趣的是,它们也存在于鞭毛虫中,这是一类单细胞异养鞭毛虫,形成后生动物的系统发育姐妹群。领鞭毛虫的一些成员能够形成短暂的群体,而其他成员则单独生活在外骨骼内。它们的分子多样性才刚刚开始显现。在这里,我们调查了 22 个领鞭毛虫物种的基因组数据,并在 16 个物种中检测到了信号蛋白/丛蛋白对。领鞭毛虫信号蛋白 (Sema-FN1) 包含几个与后生动物信号蛋白不同的结构域特征,包括可能促进二聚体稳定的 N 端 Reeler 结构域、一系列纤连蛋白 III 型结构域、一个富含丝氨酸/苏氨酸的可变结构域(是 O 连接糖基化的潜在位点)以及一个可以进行自蛋白水解的 SEA 结构域。相比之下,领鞭毛虫丛蛋白 (Plexin-1) 的结构域排列与后生动物丛蛋白基本相同。 Sema-FN1 和 Plexin-1 在 C 末端附近还包含一个短同源基序,可能与共享功能相关。三维分子模型揭示了与后生动物丛蛋白相比,领鞭毛虫 Plexin-1 具有高度保守的结构体系,包括参与细胞内 Ras-GAP 结构域激活的片段中类似的预测构象变化。几种领鞭毛虫物种中信号蛋白和丛蛋白的缺乏似乎与单细胞与群体生活方式或生态因素(例如淡水与咸水环境)无关。总之,我们的研究结果支持了信号蛋白/丛蛋白在调节单细胞和多细胞生物体细胞骨架动力学方面的保守机制。
Semaphorins and plexins are cell surface ligand/receptor proteins that affect cytoskeletal dynamics in metazoan cells. Interestingly, they are also present in Choanoflagellata, a class of unicellular heterotrophic flagellates that forms the phylogenetic sister group to Metazoa. Several members of choanoflagellates are capable of forming transient colonies, whereas others reside solitary inside exoskeletons; their molecular diversity is only beginning to emerge. Here, we surveyed genomics data from 22 choanoflagellate species and detected semaphorin/plexin pairs in 16 species. Choanoflagellate semaphorins (Sema-FN1) contain several domain features distinct from metazoan semaphorins, including an N-terminal Reeler domain that may facilitate dimer stabilization, an array of fibronectin type III domains, a variable serine/threonine-rich domain that is a potential site for O-linked glycosylation, and a SEA domain that can undergo autoproteolysis. In contrast, choanoflagellate plexins (Plexin-1) harbor a domain arrangement that is largely identical to metazoan plexins. Both Sema-FN1 and Plexin-1 also contain a short homologous motif near the C-terminus, likely associated with a shared function. Three-dimensional molecular models revealed a highly conserved structural architecture of choanoflagellate Plexin-1 as compared to metazoan plexins, including similar predicted conformational changes in a segment that is involved in the activation of the intracellular Ras-GAP domain. The absence of semaphorins and plexins in several choanoflagellate species did not appear to correlate with unicellular versus colonial lifestyle or ecological factors such as fresh versus salt water environment. Together, our findings support a conserved mechanism of semaphorin/plexin proteins in regulating cytoskeletal dynamics in unicellular and multicellular organisms.
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DOI: 10.1098/rsta.2013.0155
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影响因子: --
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