QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

Help viewing high resolution images Return to article

Fig. 5. Differential distribution of wild-type and GTPase mutant Dyn2 spliced variants. (Top) Cartoon of the Dyn2 protein showing the tripartite GTP-binding motif (yellow) and the substitution/deletion sequences of the distinct spliced variants. Red lettering indicates amino acids that differ between the `a' and `b' Dyn2 spliced variants in the first splicing cassette. Other domains of the Dyn2 protein indicated are the pleckstrin homology domain (PH), guanine nucleotide exchange domain (GED) and proline-rich domain (PRD). (A,B,C) Fluorescence micrographs of Clone 9 cells expressing GFP-tagged wild-type (WT) versions of the indicated Dyn2 spliced variants (green) that were fixed and immunostained for clathrin (red). The different Dyn2 spliced variants show varying degrees of association with clathrin, both at the plasma membrane (insets) and at the perinuclear Golgi region (arrows). (A',B',C') Fluorescence micrographs of Clone 9 cells expressing untagged GTPase mutant (K44A) versions of the different Dyn2 spliced variants that were fixed and immunostained with anti-pan-dynamin (MC63, red) and anti-clathrin (green) antibodies. Two distinct phenotypes were generally observed, including either a perinuclear concentration of mutant Dyn2 protein (A',C', arrows) or long, linear, tubular structures terminating in a prominent clathrincoated tip (B'; arrowheads in inset). (*) Indicates a transfected cell. Bars, 10 µm.

Return to article