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Figure 1.
Figure 1: Epsin 1 ENTH domain tubulates liposomes. a, Modular
arrangement of endocytic proteins. The epsin family can be
recognized by the presence of an N-terminal lipid-binding ENTH
domain and a clathrin/adaptor-binding domain. The ENTH domain is
homologous over the first 150 residues to the ANTH domains of
AP180, CALM and HIP1, although the lipid-binding residues are
very different (see Fig. 2d). The ENTH domain is followed by
ubiquitin-interacting motifs. The adaptor-binding motifs in
epsin 1 (eight DPW motifs) and DPF-like motifs in other
endocytic proteins bind to the appendage domains of the AP2
complex25. NPF motifs at the C terminus of epsin 1 interact with
the Eps15 homology (EH) domain of Eps15 (refs 7 -9). The scale
bar is in amino acid residues. b, Electron microscopy of
liposomes in the presence of the domains indicated. dAmphN,
Drosophila amphiphysin N-terminus26. The outer diameter of
tubules formed with epsin ENTH domain was 15  1
nm, that of tubules formed with full-length epsin was 19 3
nm, and that in the presence of dAmphN was 46 2
nm.
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