RRC ID 59814
Author Fujimoto K, Tanaka M, Rana AYKMM, Jahan MGS, Itoh G, Tsujioka M, Uyeda TQP, Miyagishima SY, Yumura S.
Title Dynamin-Like Protein B of Dictyostelium Contributes to Cytokinesis Cooperatively with Other Dynamins.
Journal Cells
Abstract 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.
Volume 8(8)
Published 2019-7-26
DOI 10.3390/cells8080781
PII cells8080781
PMID 31357517
PMC PMC6721605
MeSH Actins / metabolism Cytokinesis* Dictyostelium / physiology* Dynamins / metabolism* Endocytosis Fluorescent Antibody Technique Humans Protein Binding Protein Transport Proteolysis Protozoan Proteins / metabolism
IF 5.656
Times Cited 1
Resource
Cellular slime molds