Abstract
Dynamin-related proteins (DRP) are large GTPases that tubulate and pinch off membranes. The Arabidopsis genome has 16 DRPs grouped into 6 subfamilies (DRP1-6). Members of DRP2 subfamily, DRP2A and DRP2B, show similar domain structure to that of dynamin, which is involved in clathrin-coated vesicle (CCV) formation during endocytosis. However, molecular function of DRP2 subfamily is unclear. To investigate whether DRP2 is related to CCV formation during endocytosis, we compared the localizations of fluorescent fusions of DRP2B with those of clathrin light chain around the plasma membrane by variable incidence angle fluorescent microscopy (VIAFM). In our VIAFM images of Arabidopsis cultured cells, the signals of green fluorescent protein-tagged DRP2B (GFP-DRP2B) were co-localized to those of monomeric Kusabira Orange-tagged clathrin light chain (mKO-CLC). Moreover, GFP-DRP2B signals appeared and accumulated to the assembly sites of mKO-CLC. These results suggest that Arabidopsis DRP2 participates in CCV formation during endocytosis.
