The RhoGAP Domain of CYK-4 Has an Essential Role in RhoA Activation
In: Current Biology, Jg. 22 (2012-02-01), Heft 3, S. 213-219
Online
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Zugriff:
Summary Cytokinesis in animal cells is mediated by a cortical actomyosin-based contractile ring. The GTPase RhoA is a critical regulator of this process as it activates both nonmuscle myosin and a nucleator of actin filaments [1]. The site at which active RhoA and its effectors accumulate is controlled by the microtubule-based spindle during anaphase [2]. ECT-2, the guanine nucleotide exchange factor (GEF) that activates RhoA during cytokinesis, is regulated by phosphorylation and subcellular localization [3–5]. ECT2 localization depends on interactions with CYK-4/MgcRacGAP, a Rho GTPase-activating protein (GAP) domain containing protein [5, 6]. Here we show that, contrary to expectations, the Rho GTPase-activating protein (GAP) domain of CYK-4 promotes activation of RhoA during cytokinesis. Furthermore, we show that the primary phenotype caused by mutations in the GAP domain of CYK-4 is not caused by ectopic activation of CED-10/Rac1 and ARX-2/Arp2. However, inhibition of CED-10/Rac1 and ARX-2/Arp2 facilitates ingression of weak cleavage furrows. These results demonstrate that a GAP domain can contribute to activation of a small GTPase. Furthermore, cleavage furrow ingression is sensitive to the balance of contractile forces and cortical tension.
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The RhoGAP Domain of CYK-4 Has an Essential Role in RhoA Activation
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Autor/in / Beteiligte Person: | Glotzer, Michael ; Longhini, Katrina M. ; Loria, Andy |
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Zeitschrift: | Current Biology, Jg. 22 (2012-02-01), Heft 3, S. 213-219 |
Veröffentlichung: | Elsevier BV, 2012 |
Medientyp: | unknown |
ISSN: | 0960-9822 (print) |
DOI: | 10.1016/j.cub.2011.12.019 |
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