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Figure 1


Fig. 1. Dictyostelium epsin. (A) Schematic representation of the structural organization of epsin from Dictyostelium (Dd), S. cerevisae (Sc), C. elegans (Ce), Drosophila (Dm) and Homo sapiens (Hs). Each has a membrane-binding ENTH domain (yellow box) as well as an unstructured C-terminal region containing motifs for binding clathrin (blue boxes), a DPF/DPW motif that binds AP2 (red oval) and an NPF for binding EH-domain-containing proteins. (B) Dictyostelium epsin binds clathrin. Amylose resin coupled to maltose binding protein (MBP) or to MBP:epsin was incubated with Dictyostelium lysate. Whole cell lysates (WCL) and fractions that did not bind (Unbound; UB) or that did bind (Bound; B) to the resin were immunoblotted for clathrin (anti-CHC) or the {alpha}-adaptin subunit of AP2 ({alpha}-AP2). (C) Confocal images (surface focal plane) of a wild-type cell expressing epsin:GFP. (C') Confocal image (middle focal plane) from the same cell. (D,E) Epsin colocalizes extensively with clathrin and AP2. Confocal images (surface focal planes) from cells expressing epsin:GFP (green) and immunostained for clathrin (D) or AP2 (E, red). Scale bars: 5 µm.





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