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Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis
Diaphanous-related formin, mDia, is an actin nucleation/polymerization factor functioning downstream of the small GTPase Rho. Although Rho is critically involved in cytokinesis, it remains elusive how Rho effectors and other regulators of cytoskeletons work together to accomplish this process. Here...
Autores principales: | , , , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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The American Society for Cell Biology
2010
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2938385/ https://www.ncbi.nlm.nih.gov/pubmed/20660154 http://dx.doi.org/10.1091/mbc.E10-04-0324 |
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author | Watanabe, Sadanori Okawa, Katsuya Miki, Takashi Sakamoto, Satoko Morinaga, Tomoko Segawa, Kohei Arakawa, Takatoshi Kinoshita, Makoto Ishizaki, Toshimasa Narumiya, Shuh |
author_facet | Watanabe, Sadanori Okawa, Katsuya Miki, Takashi Sakamoto, Satoko Morinaga, Tomoko Segawa, Kohei Arakawa, Takatoshi Kinoshita, Makoto Ishizaki, Toshimasa Narumiya, Shuh |
author_sort | Watanabe, Sadanori |
collection | PubMed |
description | Diaphanous-related formin, mDia, is an actin nucleation/polymerization factor functioning downstream of the small GTPase Rho. Although Rho is critically involved in cytokinesis, it remains elusive how Rho effectors and other regulators of cytoskeletons work together to accomplish this process. Here we focused on mDia2, an mDia isoform involved in cytokinesis of NIH 3T3 cells, and analyzed mechanisms of its localization in cytokinesis. We found that targeting of mDia2 to the cleavage furrow requires not only its binding to RhoA but also its diaphanous-inhibitory domain (DID). We then performed pulldown assays using a fragment containing the latter domain as a bait and identified anillin as a novel mDia2 interaction partner. The anillin-binding is competitive with the diaphanous autoregulatory domain (DAD) of mDia2 in its autoinhibitory interaction. A series of RNA interference and functional rescue experiments has revealed that, in addition to the Rho GTPase-mediated activation, the interaction between mDia2 and anillin is required for the localization and function of mDia2 in cytokinesis. |
format | Text |
id | pubmed-2938385 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29383852010-11-30 Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis Watanabe, Sadanori Okawa, Katsuya Miki, Takashi Sakamoto, Satoko Morinaga, Tomoko Segawa, Kohei Arakawa, Takatoshi Kinoshita, Makoto Ishizaki, Toshimasa Narumiya, Shuh Mol Biol Cell Articles Diaphanous-related formin, mDia, is an actin nucleation/polymerization factor functioning downstream of the small GTPase Rho. Although Rho is critically involved in cytokinesis, it remains elusive how Rho effectors and other regulators of cytoskeletons work together to accomplish this process. Here we focused on mDia2, an mDia isoform involved in cytokinesis of NIH 3T3 cells, and analyzed mechanisms of its localization in cytokinesis. We found that targeting of mDia2 to the cleavage furrow requires not only its binding to RhoA but also its diaphanous-inhibitory domain (DID). We then performed pulldown assays using a fragment containing the latter domain as a bait and identified anillin as a novel mDia2 interaction partner. The anillin-binding is competitive with the diaphanous autoregulatory domain (DAD) of mDia2 in its autoinhibitory interaction. A series of RNA interference and functional rescue experiments has revealed that, in addition to the Rho GTPase-mediated activation, the interaction between mDia2 and anillin is required for the localization and function of mDia2 in cytokinesis. The American Society for Cell Biology 2010-09-15 /pmc/articles/PMC2938385/ /pubmed/20660154 http://dx.doi.org/10.1091/mbc.E10-04-0324 Text en © 2010 by The American Society for Cell Biology This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). |
spellingShingle | Articles Watanabe, Sadanori Okawa, Katsuya Miki, Takashi Sakamoto, Satoko Morinaga, Tomoko Segawa, Kohei Arakawa, Takatoshi Kinoshita, Makoto Ishizaki, Toshimasa Narumiya, Shuh Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title | Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title_full | Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title_fullStr | Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title_full_unstemmed | Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title_short | Rho and Anillin-dependent Control of mDia2 Localization and Function in Cytokinesis |
title_sort | rho and anillin-dependent control of mdia2 localization and function in cytokinesis |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2938385/ https://www.ncbi.nlm.nih.gov/pubmed/20660154 http://dx.doi.org/10.1091/mbc.E10-04-0324 |
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