A GAP that Divides.
A GAP that Divides.
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DOI：
10.12688/f1000research.12064.1
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发表时间：
2017-01-01
期刊：
影响因子：
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通讯作者：
Glotzer, Michael
中科院分区：
文献类型：
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作者：
Basant, Angika;Glotzer, Michael
后生动物细胞中的胞质分裂由肌动球蛋白为基础的收缩环介导，该收缩环响应于小G T β RhoA的激活而组装。在胞质分裂过程中激活RhoA的鸟嘌呤核苷酸交换因子ECT-2受到高度调节。在大多数后生动物细胞中，除了秀丽隐杆线虫早期胚胎的显著例外，RhoA激活和沟内陷需要centralspindlin复合物。这种例外是由于在C.优美的Centralspindlin含有CYK-4，其含有预测的Rho家族GTP酶激活蛋白（GAP）结构域。这一领域的功能一直是相当多的辩论的主题。一些出版物表明差距域促进RhoA活化（例如，Zhang和Glotzer，2015; Loria，Longhini和Glotzer，2012），而其他出版物表明其功能是抑制GTCRac 1（例如，Zhuravlev et al.，2017年）。在这里，我们回顾了胞质分裂过程中RhoA激活的机制，主要集中在C。优美的我们强调的重要性，考虑RhoA激活和详细分析CYK-4突变表型的平行途径时，评估的差距域的CYK-4的作用。
Cytokinesis in metazoan cells is mediated by an actomyosin-based contractile ring that assembles in response to activation of the small GTPase RhoA. The guanine nucleotide exchange factor that activates RhoA during cytokinesis, ECT-2, is highly regulated. In most metazoan cells, with the notable exception of the early Caenorhabditis elegans embryo, RhoA activation and furrow ingression require the centralspindlin complex. This exception is due to the existence of a parallel pathway for RhoA activation in C. elegans. Centralspindlin contains CYK-4 which contains a predicted Rho family GTPase-activating protein (GAP) domain. The function of this domain has been the subject of considerable debate. Some publications suggest that the GAP domain promotes RhoA activation (for example, Zhang and Glotzer, 2015; Loria, Longhini and Glotzer, 2012), whereas others suggest that it functions to inactivate the GTPase Rac1 (for example, Zhuravlev et al., 2017). Here, we review the mechanisms underlying RhoA activation during cytokinesis, primarily focusing on data in C. elegans. We highlight the importance of considering the parallel pathway for RhoA activation and detailed analyses of cyk-4 mutant phenotypes when evaluating the role of the GAP domain of CYK-4.