Cited by 86Microtubule and mitosis dynamicsProtein Kinase Regulation and GTPase SignalingCellular Mechanics and Interactions

An anillin-Ect2 complex stabilizes central spindle microtubules at the cortex during cytokinesis

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Frenette, Paul, Haines, Eric, Loloyan, Michael, Kinal, Mena, Pakarian, Paknoosh, Piekny, Alisa·2012·PLoS ONE

Abstract

Cytokinesis occurs due to the RhoA-dependent ingression of an actomyosin ring. During anaphase, the Rho GEF (guanine nucleotide exchange factor) Ect2 is recruited to the central spindle via its interaction with MgcRacGAP/Cyk-4, and activates RhoA in the central plane of the cell. Ect2 also localizes to the cortex, where it has access to RhoA. The N-terminus of Ect2 binds to Cyk-4, and the C-terminus contains conserved DH (Dbl homologous) and PH (Pleckstrin Homology) domains with GEF activity. The PH domain is required for Ect2's cortical localization, but its molecular function is not known. In cultured human cells, we found that the PH domain interacts with anillin, a contractile ring protein that scaffolds actin and myosin and interacts with RhoA. The anillin-Ect2 interaction may require Ect2's association with lipids, since a novel mutation in the PH domain, which disrupts phospholipid association, weakens their interaction. An anillin-RacGAP50C (homologue of Cyk-4) complex was previously described in Drosophila, which may crosslink the central spindle to the cortex to stabilize the position of the contractile ring. Our data supports an analogous function for the anillin-Ect2 complex in human cells and one hypothesis is that this complex has functionally replaced the Drosophila anillin-RacGAP50C complex. Complexes between central spindle proteins and cortical proteins could regulate the position of the contractile ring by stabilizing microtubule-cortical interactions at the division plane to ensure the generation of active RhoA in a discrete zone.

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Authors
Frenette, P., Haines, E., Loloyan, M., Kinal, M., Pakarian, P., & Piekny, A.
Affiliations
Concordia University (CA)
Corresponding author
Piekny, Alisa
Venue
PLoS ONE
Published
2012-04-13
Volume
7
Issue
4
Pages
e34888
ISSN
1932-6203 (ISSN-L)
OpenAlex
W1998737998
Cited by
86
References
46
Citations by year
2026: 2 · 2025: 4 · 2024: 3 · 2023: 1 · 2022: 9 · 2021: 7 · 2020: 8 · 2019: 6 · 2018: 5 · 2017: 8 · 2016: 4 · 2015: 10 · 2014: 9 · 2013: 6 · 2012: 4
FWCI
4.39
Type
journal article
Language
en
Open access
Locations
  • PLoS ONE (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • Spectrum Research Repository (Concordia University) (acceptedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Figshare (submittedVersion, cc-by)
Funders
Canadian Institutes of Health Research
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
cytokinesis, anillin, ECT2, central spindle, microtubules, cortex, RhoA, actomyosin ring, contractile ring, pleckstrin homology domain, phospholipid binding, Dbl homology domain, cell division plane
MeSH terms
Animals, Cell Line, Contractile Proteins, Drosophila, Fluorescent Antibody Technique, HeLa Cells, Humans, Microtubules, Spindle Apparatus, Protein Binding, Proto-Oncogene Proteins, Guanine Nucleotide Exchange Factors, Drosophila Proteins, RNA Interference, Cytokinesis

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