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- W2760933211 abstract "<ns4:p>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<ns4:italic>Caenorhabditis elegans</ns4:italic>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<ns4:italic>C. elegans</ns4:italic>. 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<ns4:italic>et al</ns4:italic>., 2017). Here, we review the mechanisms underlying RhoA activation during cytokinesis, primarily focusing on data in<ns4:italic>C. elegans.</ns4:italic>We highlight the importance of considering the parallel pathway for RhoA activation and detailed analyses of <ns4:italic>cyk-4</ns4:italic>mutant phenotypes when evaluating the role of the GAP domain of CYK-4.</ns4:p>" @default.
- W2760933211 created "2017-10-20" @default.
- W2760933211 creator A5029032834 @default.
- W2760933211 creator A5087230031 @default.
- W2760933211 date "2017-10-02" @default.
- W2760933211 modified "2023-09-24" @default.
- W2760933211 title "A GAP that Divides" @default.
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- W2760933211 doi "https://doi.org/10.12688/f1000research.12064.1" @default.
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