Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins
Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, <i>Dictyostelium discoideum</i>, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. DymA, dlpA, or dlpB-deficient cell...
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doaj-4e4e4b201ebf446fb53d5afd210ce3822020-11-25T01:12:13ZengMDPI AGCells2073-44092019-07-018878110.3390/cells8080781cells8080781Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other DynaminsKoushiro Fujimoto0Masahito Tanaka1A.Y. K. Md. Masud Rana2Md. Golam Sarowar Jahan3Go Itoh4Masatsune Tsujioka5Taro Q. P. Uyeda6Shin-ya Miyagishima7Shigehiko Yumura8Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, JapanGraduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, JapanGraduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, JapanGraduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, JapanDepartment of Molecular Medicine and Biochemistry, Akita University Graduate School of Medicine, Akita 010-8543, JapanDepartment of Pathological Cell Biology, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, JapanDepartment of Physics, Faculty of Science and Technology, Waseda University, Tokyo 169-8555, JapanDepartment of Gene Function and Phenomics, Center for Frontier Research, National Institute of Genetics, Shizuoka 411-8540, JapanGraduate School of Sciences and Technology for Innovation, Yamaguchi University, Yamaguchi 753-8511, JapanDynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, <i>Dictyostelium discoideum</i>, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. DymA, dlpA, or dlpB-deficient cells exhibited defects in cytokinesis. DlpA and dlpB were found to colocalize at cleavage furrows from the early phase, and dymA localized at the intercellular bridge connecting the two daughter cells, indicating that these dynamins contribute to cytokinesis at distinct dividing stages. Total internal reflection fluorescence microscopy revealed that dlpA and dlpB colocalized at individual dots at the furrow cortex. However, dlpA and dlpB did not colocalize with clathrin, suggesting that they are not involved in clathrin-mediated endocytosis. The fact that dlpA did not localize at the furrow in dlpB null cells and vice versa, as well as other several lines of evidence, suggests that hetero-oligomerization of dlpA and dlpB is required for them to bind to the furrow. The hetero-oligomers directly or indirectly associate with actin filaments, stabilizing them in the contractile rings. Interestingly, dlpA, but not dlpB, accumulated at the phagocytic cups independently of dlpB. Our results suggest that the hetero-oligomers of dlpA and dlpB contribute to cytokinesis cooperatively with dymA.https://www.mdpi.com/2073-4409/8/8/781actincontractile ringcytokinesisdynaminendocytosis |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Koushiro Fujimoto Masahito Tanaka A.Y. K. Md. Masud Rana Md. Golam Sarowar Jahan Go Itoh Masatsune Tsujioka Taro Q. P. Uyeda Shin-ya Miyagishima Shigehiko Yumura |
spellingShingle |
Koushiro Fujimoto Masahito Tanaka A.Y. K. Md. Masud Rana Md. Golam Sarowar Jahan Go Itoh Masatsune Tsujioka Taro Q. P. Uyeda Shin-ya Miyagishima Shigehiko Yumura Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins Cells actin contractile ring cytokinesis dynamin endocytosis |
author_facet |
Koushiro Fujimoto Masahito Tanaka A.Y. K. Md. Masud Rana Md. Golam Sarowar Jahan Go Itoh Masatsune Tsujioka Taro Q. P. Uyeda Shin-ya Miyagishima Shigehiko Yumura |
author_sort |
Koushiro Fujimoto |
title |
Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins |
title_short |
Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins |
title_full |
Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins |
title_fullStr |
Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins |
title_full_unstemmed |
Dynamin-Like Protein B of <i>Dictyostelium</i> Contributes to Cytokinesis Cooperatively with Other Dynamins |
title_sort |
dynamin-like protein b of <i>dictyostelium</i> contributes to cytokinesis cooperatively with other dynamins |
publisher |
MDPI AG |
series |
Cells |
issn |
2073-4409 |
publishDate |
2019-07-01 |
description |
Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, <i>Dictyostelium discoideum</i>, has five dynamin-like proteins: dymA, dymB, dlpA, dlpB, and dlpC. DymA, dlpA, or dlpB-deficient cells exhibited defects in cytokinesis. DlpA and dlpB were found to colocalize at cleavage furrows from the early phase, and dymA localized at the intercellular bridge connecting the two daughter cells, indicating that these dynamins contribute to cytokinesis at distinct dividing stages. Total internal reflection fluorescence microscopy revealed that dlpA and dlpB colocalized at individual dots at the furrow cortex. However, dlpA and dlpB did not colocalize with clathrin, suggesting that they are not involved in clathrin-mediated endocytosis. The fact that dlpA did not localize at the furrow in dlpB null cells and vice versa, as well as other several lines of evidence, suggests that hetero-oligomerization of dlpA and dlpB is required for them to bind to the furrow. The hetero-oligomers directly or indirectly associate with actin filaments, stabilizing them in the contractile rings. Interestingly, dlpA, but not dlpB, accumulated at the phagocytic cups independently of dlpB. Our results suggest that the hetero-oligomers of dlpA and dlpB contribute to cytokinesis cooperatively with dymA. |
topic |
actin contractile ring cytokinesis dynamin endocytosis |
url |
https://www.mdpi.com/2073-4409/8/8/781 |
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