Cited by 426Microtubule and mitosis dynamicsProtein Kinase Regulation and GTPase SignalingCellular Mechanics and Interactions

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Anillin Is a Scaffold Protein That Links RhoA, Actin, and Myosin during Cytokinesis

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Piekny, Alisa J., Glotzer, Michael·2008·Current Biology

DOI 10.1016/j.cub.2007.11.068

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Abstract

Cell division after mitosis is mediated by ingression of an actomyosin-based contractile ring. The active, GTP-bound form of the small GTPase RhoA is a key regulator of contractile-ring formation. RhoA concentrates at the equatorial cell cortex at the site of the nascent cleavage furrow. During cytokinesis, RhoA is activated by its RhoGEF, ECT2. Once activated, RhoA promotes nucleation, elongation, and sliding of actin filaments through the coordinated activation of both formin proteins and myosin II motors (reviewed in [1, 2]). Anillin is a 124 kDa protein that is highly concentrated in the cleavage furrow in numerous animal cells in a pattern that resembles that of RhoA [3-7]. Although anillin contains conserved N-terminal actin and myosin binding domains and a PH domain at the C terminus, its mechanism of action during cytokinesis remains unclear. Here, we show that human anillin contains a conserved C-terminal domain that is essential for its function and localization. This domain shares homology with the RhoA binding protein Rhotekin and directly interacts with RhoA. Further, anillin is required to maintain active myosin in the equatorial plane during cytokinesis, suggesting it functions as a scaffold protein to link RhoA with the ring components actin and myosin. Although furrows can form and initiate ingression in the absence of anillin, furrows cannot form in anillin-depleted cells in which the central spindle is also disrupted, revealing that anillin can also act at an early stage of cytokinesis.

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Authors: Piekny, A. J., & Glotzer, M.
Affiliations: University of Chicago (US)
Corresponding author: Glotzer, Michael
ORCID: Piekny, Alisa J.
Glotzer, Michael
Venue: Current Biology
Publisher: Elsevier BV
Published: 2008-01
Volume: 18
Issue: 1
Pages: 30-36
ISSN: 0960-9822 (ISSN-L)
DOI: 10.1016/j.cub.2007.11.068
OpenAlex: W2049863303
Cited by: 426
References: 28
Citations by year: 2026: 8 · 2025: 12 · 2024: 20 · 2023: 29 · 2022: 34 · 2021: 30 · 2020: 37 · 2019: 26 · 2018: 24 · 2017: 29 · 2016: 33 · 2015: 26 · 2014: 19 · 2013: 18 · 2012: 16
FWCI: 9.48
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2060 d)
doi.org/10.15223/policy-017 (stm-asf)
doi.org/10.15223/policy-037 (stm-asf)
doi.org/10.15223/policy-012 (stm-asf)
doi.org/10.15223/policy-029 (stm-asf)
doi.org/10.15223/policy-004 (stm-asf)
Locations: Current Biology (publishedVersion)
PubMed (publishedVersion)
Funders: Canadian Institutes of Health Research
National Institutes of Health (GM074743-01)
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: anillin, cytokinesis, RhoA, contractile ring, cleavage furrow, myosin II, actomyosin, scaffold proteins, Rhotekin, central spindle, actin, formins, cell division
MeSH terms: Actins, Amino Acid Sequence, Contractile Proteins, HeLa Cells, Humans, Spindle Apparatus, Molecular Sequence Data, Myosins, Sequence Alignment, Conserved Sequence, Protein Structure, Tertiary, GTP-Binding Proteins, rhoA GTP-Binding Protein, Intracellular Signaling Peptides and Proteins, Cytokinesis, Apoptosis Regulatory Proteins

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Anillin Is a Scaffold Protein That Links RhoA, Actin, and Myosin during Cytokinesis

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