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Cited by 208Microtubule and mitosis dynamicsProtein Kinase Regulation and GTPase SignalingCellular Mechanics and Interactions

MgcRacGAP controls the assembly of the contractile ring and the initiation of cytokinesis

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Zhao, Wei-meng, Fang, Guowei·2005·Proceedings of the National Academy of Sciences
DOI 10.1073/pnas.0504145102PMC PMC1201590
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Abstract

Initiation of cytokinesis requires the establishment of the cleavage plane, the assembly of the contractile ring, and the ingression of the cleavage furrow. MgcRacGAP, a GTPase-activating protein for RhoA, is required for cytokinesis, but the mechanism of its action remains unknown. We report here that MgcRacGAP is required for the assembly of anillin and myosin into the contractile ring. In addition, MgcRacGAP is required for the localized activation of myosin through the RhoA-mediated phosphorylation of the myosin regulatory light chain. Cells with MgcRacGAP RNA interference (RNAi) failed cytokinesis without any ingression of the cleavage furrow. Paradoxically, MgcRacGAP, a GTPase-activating protein, associates during cytokinesis with ECT2, a guanine nucleotide exchange factor for RhoA, and the localization of ECT2 to both the central spindle and the contractile ring depends on MgcRacGAP. Knockdown of ECT2 phenocopies that of MgcRacGAP. We conclude that MgcRacGAP controls the initiation of cytokinesis by regulating ECT2, which in turn induces the assembly of the contractile ring and triggers the ingression of the cleavage furrow.

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  • RACGAP1 is a GAP that spatially and temporally activates Rac and RhoA to regulate Jnk and Yap signaling as well as cell division.

    “and a GAP that spatially and temporally activates Rac and RhoA to regulate Jnk and Yap signaling as well as cell division.”

    From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [90]

    The Results and Discussion (page numbers unavailable) support a role for MgcRacGAP in RhoA localization and the initiation of cytokinesis. The Discussion describes ECT2—not MgcRacGAP directly—as a positive regulator of RhoA, and the cited passages do not support activation of Rac or regulation of Jnk or Yap signaling. (LLM, conf=0.89)

    Experimental — accuracy not yet measured

  • RACGAP1 is a component of the centralspindlin complex.

    “Rac GTPase-activating protein 1 (RACGAP1, also known as MgcRacGAP/CYK4) is a component of the centralspindlin complex”

    From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [90]

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Authors
Zhao, W.-M., & Fang, G.
Affiliations
Stanford University (US)
Venue
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences
Published
2005-08-29
Volume
102
Issue
37
Pages
13158-13163
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
DOI
10.1073/pnas.0504145102
PMC
PMC1201590
OpenAlex
W2123924160
Cited by
208
References
0
Citations by year
2026: 2 · 2025: 6 · 2024: 13 · 2023: 4 · 2022: 13 · 2021: 5 · 2020: 8 · 2019: 4 · 2018: 4 · 2017: 5 · 2016: 12 · 2015: 9 · 2014: 15 · 2013: 10 · 2012: 20
FWCI
4.94
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of General Medical Sciences (R01GM062852, GM-062852)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords
MgcRacGAP, contractile ring assembly, RhoA, GTPase-activating protein, ECT2, guanine nucleotide exchange factor, myosin regulatory light chain phosphorylation, anillin, cleavage planes, central spindle, cell division
MeSH terms
Contractile Proteins, Cytoskeleton, HeLa Cells, Humans, Spindle Apparatus, Myosins, Proto-Oncogene Proteins, Transfection, Myosin Light Chains, GTPase-Activating Proteins, rhoA GTP-Binding Protein, RNA, Small Interfering, Cytokinesis

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