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Stabilization of the actomyosin ring enables spermatocyte cytokinesis in Drosophila.
Mol Biol Cell. 2010 May 01; 21(9):1482-93.MB

Abstract

The scaffolding protein anillin is required for completion of cytokinesis. Anillin binds filamentous (F) actin, nonmuscle myosin II, and septins and in cell culture models has been shown to restrict actomyosin contractility to the cleavage furrow. Whether anillin also serves this function during the incomplete cytokinesis that occurs in developing germ cells has remained unclear. Here, we show that anillin is required for cytokinesis in dividing Drosophila melanogaster spermatocytes and that anillin, septins, and myosin II stably associate with the cleavage furrow in wild-type cells. Anillin is necessary for recruitment of septins to the cleavage furrow and for maintenance of F-actin and myosin II at the equator in late stages of cytokinesis. Remarkably, expression of DE-cadherin suppresses the cytokinesis defect of anillin-depleted spermatocytes. DE-cadherin recruits beta-catenin (armadillo) and alpha-catenin to the cleavage furrow and stabilizes F-actin at the equator. Similarly, E-cadherin expression suppresses the cytokinesis defect caused by anillin knockdown in mouse L-fibroblast cells. Our results show that the anillin-septin and cadherin-catenin complexes can serve as alternative cassettes to promote tight physical coupling of F-actin and myosin II to the cleavage furrow and successful completion of cytokinesis.

Authors+Show Affiliations

Program in Developmental and Stem Cell Biology, The Hospital for Sick Children, Toronto, ON, M5G 1L7, Canada.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20237160

Citation

Goldbach, Philip, et al. "Stabilization of the Actomyosin Ring Enables Spermatocyte Cytokinesis in Drosophila." Molecular Biology of the Cell, vol. 21, no. 9, 2010, pp. 1482-93.
Goldbach P, Wong R, Beise N, et al. Stabilization of the actomyosin ring enables spermatocyte cytokinesis in Drosophila. Mol Biol Cell. 2010;21(9):1482-93.
Goldbach, P., Wong, R., Beise, N., Sarpal, R., Trimble, W. S., & Brill, J. A. (2010). Stabilization of the actomyosin ring enables spermatocyte cytokinesis in Drosophila. Molecular Biology of the Cell, 21(9), 1482-93. https://doi.org/10.1091/mbc.E09-08-0714
Goldbach P, et al. Stabilization of the Actomyosin Ring Enables Spermatocyte Cytokinesis in Drosophila. Mol Biol Cell. 2010 May 1;21(9):1482-93. PubMed PMID: 20237160.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Stabilization of the actomyosin ring enables spermatocyte cytokinesis in Drosophila. AU - Goldbach,Philip, AU - Wong,Raymond, AU - Beise,Nolan, AU - Sarpal,Ritu, AU - Trimble,William S, AU - Brill,Julie A, Y1 - 2010/03/17/ PY - 2010/3/19/entrez PY - 2010/3/20/pubmed PY - 2010/8/21/medline SP - 1482 EP - 93 JF - Molecular biology of the cell JO - Mol Biol Cell VL - 21 IS - 9 N2 - The scaffolding protein anillin is required for completion of cytokinesis. Anillin binds filamentous (F) actin, nonmuscle myosin II, and septins and in cell culture models has been shown to restrict actomyosin contractility to the cleavage furrow. Whether anillin also serves this function during the incomplete cytokinesis that occurs in developing germ cells has remained unclear. Here, we show that anillin is required for cytokinesis in dividing Drosophila melanogaster spermatocytes and that anillin, septins, and myosin II stably associate with the cleavage furrow in wild-type cells. Anillin is necessary for recruitment of septins to the cleavage furrow and for maintenance of F-actin and myosin II at the equator in late stages of cytokinesis. Remarkably, expression of DE-cadherin suppresses the cytokinesis defect of anillin-depleted spermatocytes. DE-cadherin recruits beta-catenin (armadillo) and alpha-catenin to the cleavage furrow and stabilizes F-actin at the equator. Similarly, E-cadherin expression suppresses the cytokinesis defect caused by anillin knockdown in mouse L-fibroblast cells. Our results show that the anillin-septin and cadherin-catenin complexes can serve as alternative cassettes to promote tight physical coupling of F-actin and myosin II to the cleavage furrow and successful completion of cytokinesis. SN - 1939-4586 UR - https://www.unboundmedicine.com/medline/citation/20237160/Stabilization_of_the_actomyosin_ring_enables_spermatocyte_cytokinesis_in_Drosophila_ L2 - https://www.molbiolcell.org/doi/10.1091/mbc.e09-08-0714?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -