The genomic underpinnings of apoptosis in Strongylocentrotus purpuratus.
The genomic underpinnings of apoptosis in Strongylocentrotus purpuratus.
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DOI：
10.1016/j.ydbio.2006.08.053
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发表时间：
2006-12
影响因子：
2.7
通讯作者：
A. Robertson;Jenifer C. Croce;S. Carbonneau;Ekaterina Voronina;Esther Miranda;D. McClay;J. Coffman
中科院分区：
文献类型：
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作者：
A. Robertson;Jenifer C. Croce;S. Carbonneau;Ekaterina Voronina;Esther Miranda;D. McClay;J. Coffman
程序性细胞死亡通过凋亡是一个泛后生动物的特点，涉及分子间的信号网络，经历了大量的谱系特异性的演变。一项对海胆基因组中编码的阿尔茨海默病相关蛋白质的调查提供了对这种进化的深入了解，同时揭示了一些有趣的新颖性，我们在这里强调。首先，除了典型的携带CARD的Apaf-1同源物外，海胆还具有至少两种新型的Apaf-1样蛋白，每种蛋白都与死亡结构域相连，这表明棘皮动物已经进化出独特的细胞凋亡信号通路。第二，海胆具有异常大量的半胱天冬酶。虽然海胆中的效应器半胱天冬酶（半胱天冬酶-3/7和半胱天冬酶-6）的集合与在其他基部后口动物中发现的相似，但信号响应性启动器半胱天冬酶亚家族（半胱天冬酶-8/10和9，其分别与DED和CARD适配器结构域连接）经历了棘皮动物特异性扩增。此外，有两组不同的半胱天冬酶，一组与脊椎动物白细胞介素转化酶（ICE）样亚家族有较远的关系，另一个大家族不与任何脊椎动物半胱天冬酶聚类。第三，含有抗凋亡BIR结构域和Bcl-2家族成员的蛋白质的复杂性接近脊椎动物的复杂性，并且大于在原口动物模型系统如果蝇或秀丽隐杆线虫中发现的复杂性。最后，死亡受体同源物的存在，以前只知道在脊椎动物中，在圆海胆purpuratus和Nematostella vectensis表明，这个家族的细胞凋亡信号蛋白在动物早期进化，随后在线虫和节肢动物谱系中丢失。我们的研究结果表明，细胞的生存是偶然的信号在海胆，更可比的复杂性脊椎动物比节肢动物或线虫，但也具有独特的功能，可能涉及到的双相生命周期和/或免疫特异性的这种生物体的具体要求。
Programmed cell death through apoptosis is a pan-metazoan character involving intermolecular signaling networks that have undergone substantial lineage-specific evolution. A survey of apoptosis-related proteins encoded in the sea urchin genome provides insight into this evolution while revealing some interesting novelties, which we highlight here. First, in addition to a typical CARD-carrying Apaf-1 homologue, sea urchins have at least two novel Apaf-1-like proteins that are each linked to a death domain, suggesting that echinoderms have evolved unique apoptotic signaling pathways. Second, sea urchins have an unusually large number of caspases. While the set of effector caspases (caspases-3/7 and caspase-6) in sea urchins is similar to that found in other basal deuterostomes, signal-responsive initiator caspase subfamilies (caspases-8/10 and 9, which are respectively linked to DED and CARD adaptor domains) have undergone echinoderm-specific expansions. In addition, there are two groups of divergent caspases, one distantly related to the vertebrate interleukin converting enzyme (ICE)-like subfamily, and a large clan that does not cluster with any of the vertebrate caspases. Third, the complexity of proteins containing an anti-apoptotic BIR domain and of Bcl-2 family members approaches that of vertebrates, and is greater than that found in protostome model systems such as Drosophila or Caenorhabditis elegans. Finally, the presence of Death receptor homologues, previously known only in vertebrates, in both Strongylocentrotus purpuratus and Nematostella vectensis suggests that this family of apoptotic signaling proteins evolved early in animals and was subsequently lost in the nematode and arthropod lineage(s). Our results suggest that cell survival is contingent upon a diverse array of signals in sea urchins, more comparable in complexity to vertebrates than to arthropods or nematodes, but also with unique features that may relate to specific requirements imposed by the biphasic life cycle and/or immunological idiosyncrasies of this organism.