Opposing roles of p190RhoGAP and Ect2 RhoGEF in regulating cytokinesis

Mikawa, Masahito; Su, Ling; Parsons, Sarah J.

doi:10.4161/cc.7.13.6128

Cited by 27 publications

(40 citation statements)

References 38 publications

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“…3) (Miller and Bement 2009). However, similar findings have not been reported in other systems and at least two other GAPs, p190RhoGAP and ARHGAP11A, have also been reported to inhibit RhoA during cell division (Mikawa et al 2008;Zanin et al 2013). Therefore, it is currently unclear whether this role of RacGAP1 is conserved.…”

Section: Cleavage Furrow Ingression: Actomyosin Filaments Take Centermentioning

confidence: 49%

Cytokinesis in Animal Cells

D’Avino

Giansanti

Petronczki

2015

Cold Spring Harb Perspect Biol

177

226

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Section: Cleavage Furrow Ingression: Actomyosin Filaments Take Centermentioning

confidence: 49%

Cytokinesis in Animal Cells

D’Avino

Giansanti

Petronczki

2015

Cold Spring Harb Perspect Biol

177

226

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“…Our previous findings suggest that mammalian cells have an additional level of RhoA regulation during cytokinetic furrow progression that is mediated by p190RhoGAP-A (also known as ARHGAP35, and hereafter called p190) (Su et al, 2003;Mikawa et al, 2008). p190 localizes to the cytokinetic furrow (Su et al, 2003), and cells ectopically expressing the protein exhibit reduced RhoA-GTP levels in the furrow and become multinucleated, supporting the idea that proper cycling of RhoA between active and inactive states is required for completion of cytokinesis .…”

Section: Introductionmentioning

confidence: 85%

“…6A,A9). That MLC II is downstream of p190 is further emphasized by the fact that the inability to complete cytokinesis due to p190 overexpression (and decreased RhoA-GTP levels) (Mikawa et al, 2008;Su et al, 2003;Su et al, 2009) can be rescued with a constitutively active MLC II. Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Anillin localizes at the cytokinetic furrow during cytokinesis. It has been shown that p190 also binds RhoA and Ect2 (Ludwig et al, 2009;Mikawa et al, 2008) and localizes to the cytokinetic furrow during all stages of cytokinesis (Su et al, 2003). Therefore, we tested whether these two proteins interact with each other.…”

Section: P190 Binds With Anillin During Cytokinesismentioning

confidence: 99%

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A complex of p190RhoGAP and anillin modulates RhoGTP and the cytokinetic furrow in human cells

Manukyan

Ludwig²,

Sanchez-Manchinelly³

et al. 2014

Journal of Cell Science

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The cytokinetic furrow (CF) is organized by the RhoA GTPase, which recruits actin and myosin II to the furrow and drives contractility. Here we show a role for the RhoGAP, p190, in cytokinesis and its involvement in regulating Rho GTP levels and contractility. Cells depleted of p190RhoGAP (p190) accumulate high levels of RhoGTP and markers of high Rho activity in the furrow, resulting in failure of the CF to progress to abscission. The loss of p190 can be rescued by a low dose of the myosin II inhibitor blebbistatin, suggesting that cells fail cytokinesis because they have too much myosin activity. p190RhoGAP binds the cytokinetic organizer anillin, and mutants of p190 that are unable to bind anillin or unable to inactivate Rho fail to rescue cytokinesis defects in p190-depleted cells. Together these data demonstrate that a complex of p190RhoGAP and anillin modulates RhoGTP levels in the CF to ensure robust cytokinesis.

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“…It has been suggested that p190, a Rho-specific GAP, and the ECT2 GEF cooperate antagonistically to regulate the activity of RhoA (the Rho1 counterpart in higher eukaryotes) during cytokinesis in human cells (Mikawa et al 2008). p190 GAP is inhibited by phosphorylation and activated by PP2A-mediated dephosphorylation (Mori et al 2009).…”

Section: Rho1 Inhibition By Pp2a-pab1mentioning

confidence: 99%

Feedback Regulation of SIN by Etd1 and Rho1 in Fission Yeast

et al. 2014

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In fission yeast, the septation initiation network (SIN) is thought to promote cytokinesis by downstream activation of Rho1, a conserved GTPase that controls cell growth and division. Here we show that Etd1 and PP2A-Pab1, antagonistic regulators of SIN, are Rho1 regulators. Our genetic and biochemical studies indicate that a C-terminal region of Etd1 may activate Rho1 by directly binding it, whereas an N-terminal domain confers its ability to localize at the growing tips and the division site where Rho1 functions. In opposition to Etd1, our results indicate that PP2A-Pab1 inhibits Rho1. The SIN cascade is upstream-regulated by the Spg1 GTPase. In the absence of Etd1, activity of Spg1 drops down prematurely, thereby inactivating SIN. Interestingly, we find that ectopic activation of Rho1 restores Spg1 activity in Etd1-depleted cells. By using a cytokinesis block strategy, we show that Rho1 is essential to feedbackactivate Spg1 during actomyosin ring constriction. Therefore, activation of Spg1 by Rho1, which in turn is regulated by Etd1, uncovers a novel feedback loop mechanism that ensures SIN activity while cytokinesis is progressing.F ISSION yeast cells grow by elongating at their cell ends before dividing by forming a medially placed division septum during cytokinesis. New-born cells initiate growth in a monopolar manner from the old cell end that existed before division. During G2, cells initiate growth from the new end in a process known as NETO (new end take-off). These cells then grow in a bipolar mode until mitosis, when they stop growth and initiate cell division by septation (Mitchison and Nurse 1985;Hayles and Nurse 2001). Both polar growth and septation require proper cell membrane and cell-wall synthesis to ensure cell integrity. In Schizosaccharomyces pombe, the cell wall is composed of b-glucan, a-glucan, and mannoproteins. Synthesis of the major cell wall and primary septum polymer, 1,3-b-glucan, requires the activity of Drc1/Cps1/Bgs1 1,3-b-glucan synthase, which in turn is regulated by the guanosine triphosphate (GTP)-binding protein Rho1 (Garcia et al. 2006;Cortes et al. 2007). As with all GTPases, Rho1 acts as a binary switch, cycling between inactive GDP-bound and active GTPbound conformational states (Yang et al. 2003). This transition is controlled by three types of proteins: GEFs (guanine exchange factors), which catalyze the exchange of GDP for GTP, rendering the protein active; GAPs (GTPase activating proteins), which enhance nucleotide hydrolysis, inactivating the GTPase; and guanine nucleotide dissociation inhibitors, which appear to block spontaneous activation (Garcia et al. 2006).Upon the onset of mitosis, growth ceases at the cell ends and is re-established in the middle of the cell, where the actomyosin ring forms. At the end of mitosis, once the two sets of chromosomes have segregated, actomyosin ring constriction and septum formation is triggered by the septation initiation network (SIN) from the spindle pole body (SPB) (Krapp et al. 2004;Wolfe and Gould 2005). The nucl...

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Opposing roles of p190RhoGAP and Ect2 RhoGEF in regulating cytokinesis

Cited by 27 publications

References 38 publications

Cytokinesis in Animal Cells

Cytokinesis in Animal Cells

A complex of p190RhoGAP and anillin modulates RhoGTP and the cytokinetic furrow in human cells

Feedback Regulation of SIN by Etd1 and Rho1 in Fission Yeast

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