Dynamin-like protein B of Dictyostelium contributes to cytokinesis cooperatively with other dynamins

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


Dynamin is a large GTPase responsible for diverse cellular processes, such as endocytosis, division of organelles, and cytokinesis. The social amoebozoan, Dictyostelium discoideum, 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.

Original languageEnglish
Article number781
Issue number8
Publication statusPublished - 2019 Aug


  • Actin
  • Contractile ring
  • Cytokinesis
  • Dynamin
  • Endocytosis

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology


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