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Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis.
Curr Biol. 2008 Jan 08; 18(1):30-6.CB

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.

Authors+Show Affiliations

Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, Illinois 60637, USA.No affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18158243

Citation

Piekny, Alisa J., and Michael Glotzer. "Anillin Is a Scaffold Protein That Links RhoA, Actin, and Myosin During Cytokinesis." Current Biology : CB, vol. 18, no. 1, 2008, pp. 30-6.
Piekny AJ, Glotzer M. Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. Curr Biol. 2008;18(1):30-6.
Piekny, A. J., & Glotzer, M. (2008). Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. Current Biology : CB, 18(1), 30-6.
Piekny AJ, Glotzer M. Anillin Is a Scaffold Protein That Links RhoA, Actin, and Myosin During Cytokinesis. Curr Biol. 2008 Jan 8;18(1):30-6. PubMed PMID: 18158243.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. AU - Piekny,Alisa J, AU - Glotzer,Michael, Y1 - 2007/12/27/ PY - 2007/09/11/received PY - 2007/11/16/revised PY - 2007/11/28/accepted PY - 2007/12/26/pubmed PY - 2008/3/28/medline PY - 2007/12/26/entrez SP - 30 EP - 6 JF - Current biology : CB JO - Curr. Biol. VL - 18 IS - 1 N2 - 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. SN - 0960-9822 UR - https://www.unboundmedicine.com/medline/citation/18158243/Anillin_is_a_scaffold_protein_that_links_RhoA_actin_and_myosin_during_cytokinesis_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0960-9822(07)02414-1 DB - PRIME DP - Unbound Medicine ER -