Related Experiment Video
Updated: Jul 5, 2026

Real-time Imaging of Plant Cell Surface Dynamics with Variable-angle Epifluorescence Microscopy
Published on: December 12, 2015
Dynamics of Arabidopsis dynamin-related protein 1C and a clathrin light chain at the plasma membrane
Catherine A Konopka1, Steven K Backues, Sebastian Y Bednarek
1Program in Cellular and Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706, USA.
Abstract:
Plant morphogenesis depends on polarized exocytic and endocytic membrane trafficking. Members of the Arabidopsis thaliana dynamin-related protein 1 (DRP1) subfamily are required for polarized cell expansion and cytokinesis. Using a combination of live-cell imaging techniques, we show that a functional DRP1C green fluorescent fusion protein (DRP1C-GFP) was localized at the division plane in dividing cells and to the plasma membrane in expanding interphase cells. In both tip growing root hairs and diffuse-polar expanding epidermal cells, DRP1C-GFP organized into dynamic foci at the cell cortex, which colocalized with a clathrin light chain fluorescent fusion protein (CLC-FFP), suggesting that DRP1C may participate in clathrin-mediated membrane dynamics. DRP1C-GFP and CLC-GFP foci dynamics are dependent on cytoskeleton organization, cytoplasmic streaming, and functional clathrin-mediated endocytic traffic. Our studies provide insight into DRP1 and clathrin dynamics in the plant cell cortex and indicate that the clathrin endocytic machinery in plants has both similarities and striking differences to that in mammalian cells and yeast.
Related Concept Videos
Clathrin Coated Vesicles
Pinching-off of Coated Vesicles
Protein Transport to the Inner Chloroplast Membrane
Coat Assembly and GTPases
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
Mechanism of Lamellipodia Formation
Protein Transport to the Thylakoids

