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Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion
Cell–cell fusion is an intriguing differentiation process, essential for placental development and maturation. A proteomic approach identified a cytoplasmic protein, calponin 3 (CNN3), related to the fusion of BeWo choriocarcinoma cells. CNN3 was expressed in cytotrophoblasts in human placenta. CNN3...
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/PMC2982094/ https://www.ncbi.nlm.nih.gov/pubmed/20861310 http://dx.doi.org/10.1091/mbc.E10-03-0261 |
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author | Shibukawa, Yukinao Yamazaki, Natsuko Kumasawa, Keiichi Daimon, Etsuko Tajiri, Michiko Okada, Yuka Ikawa, Masahito Wada, Yoshinao |
author_facet | Shibukawa, Yukinao Yamazaki, Natsuko Kumasawa, Keiichi Daimon, Etsuko Tajiri, Michiko Okada, Yuka Ikawa, Masahito Wada, Yoshinao |
author_sort | Shibukawa, Yukinao |
collection | PubMed |
description | Cell–cell fusion is an intriguing differentiation process, essential for placental development and maturation. A proteomic approach identified a cytoplasmic protein, calponin 3 (CNN3), related to the fusion of BeWo choriocarcinoma cells. CNN3 was expressed in cytotrophoblasts in human placenta. CNN3 gene knockdown promoted actin cytoskeletal rearrangement and syncytium formation in BeWo cells, suggesting CNN3 to be a negative regulator of trophoblast fusion. Indeed, CNN3 depletion promoted BeWo cell fusion. CNN3 at the cytoplasmic face of cytoskeleton was dislocated from F-actin with forskolin treatment and diffused into the cytoplasm in a phosphorylation-dependent manner. Phosphorylation sites were located at Ser293/296 in the C-terminal region, and deletion of this region or site-specific disruption of Ser293/296 suppressed syncytium formation. These CNN3 mutants were colocalized with F-actin and remained there after forskolin treatment, suggesting that dissociation of CNN3 from F-actin is modulated by the phosphorylation status of the C-terminal region unique to CNN3 in the CNN family proteins. The mutant missing these phosphorylation sites displayed a dominant negative effect on cell fusion, while replacement of Ser293/296 with aspartic acid enhanced syncytium formation. These results indicated that CNN3 regulates actin cytoskeleton rearrangement which is required for the plasma membranes of trophoblasts to become fusion competent. |
format | Text |
id | pubmed-2982094 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2010 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-29820942011-01-30 Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion Shibukawa, Yukinao Yamazaki, Natsuko Kumasawa, Keiichi Daimon, Etsuko Tajiri, Michiko Okada, Yuka Ikawa, Masahito Wada, Yoshinao Mol Biol Cell Articles Cell–cell fusion is an intriguing differentiation process, essential for placental development and maturation. A proteomic approach identified a cytoplasmic protein, calponin 3 (CNN3), related to the fusion of BeWo choriocarcinoma cells. CNN3 was expressed in cytotrophoblasts in human placenta. CNN3 gene knockdown promoted actin cytoskeletal rearrangement and syncytium formation in BeWo cells, suggesting CNN3 to be a negative regulator of trophoblast fusion. Indeed, CNN3 depletion promoted BeWo cell fusion. CNN3 at the cytoplasmic face of cytoskeleton was dislocated from F-actin with forskolin treatment and diffused into the cytoplasm in a phosphorylation-dependent manner. Phosphorylation sites were located at Ser293/296 in the C-terminal region, and deletion of this region or site-specific disruption of Ser293/296 suppressed syncytium formation. These CNN3 mutants were colocalized with F-actin and remained there after forskolin treatment, suggesting that dissociation of CNN3 from F-actin is modulated by the phosphorylation status of the C-terminal region unique to CNN3 in the CNN family proteins. The mutant missing these phosphorylation sites displayed a dominant negative effect on cell fusion, while replacement of Ser293/296 with aspartic acid enhanced syncytium formation. These results indicated that CNN3 regulates actin cytoskeleton rearrangement which is required for the plasma membranes of trophoblasts to become fusion competent. The American Society for Cell Biology 2010-11-15 /pmc/articles/PMC2982094/ /pubmed/20861310 http://dx.doi.org/10.1091/mbc.E10-03-0261 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 Shibukawa, Yukinao Yamazaki, Natsuko Kumasawa, Keiichi Daimon, Etsuko Tajiri, Michiko Okada, Yuka Ikawa, Masahito Wada, Yoshinao Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title | Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title_full | Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title_fullStr | Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title_full_unstemmed | Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title_short | Calponin 3 Regulates Actin Cytoskeleton Rearrangement in Trophoblastic Cell Fusion |
title_sort | calponin 3 regulates actin cytoskeleton rearrangement in trophoblastic cell fusion |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2982094/ https://www.ncbi.nlm.nih.gov/pubmed/20861310 http://dx.doi.org/10.1091/mbc.E10-03-0261 |
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