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Figure 1


Fig. 1. Mosquito ARH-like orthologues. (A) Schematic of the domain organization of human (Hs), Xenopus laevis (Xl), A. gambiae (Ag) and A. aegypti (Aa) ARH and ARH-like proteins. The location of clathrin- (red) and AP-2 β2- (green) or putative {alpha}-appendage-binding (blue) interaction motifs is shown. (B) Sequence alignment of the PTB-domain regions of D. melanogaster (Dm) Numb (FlyBase Gene ID CG3779; PBD accession number: 1DDM), human ARH and Anopheles and Aedes ARH-like proteins. Numbered secondary structure elements ({alpha} helix, blue; β-strand, green) of the Numb PTB domain are indicated above. Identical residues (magenta) and chemically conservative substitutions (yellow) are boxed. Positionally conserved basic residues that, based on the structures of the Dab1 and Dab2 PTB domains, are probably involved in phosphoinositide binding (vertical arrowheads) and in FXNPXY-sequence engagement (vertical arrows) are indicated. (C) Sequence alignment of the C-terminal portions of the Anopheles, Aedes and Tribolium castaneum (Tc) ARH-like proteins. Conservation colored as in B and the location of the putative clathrin (red) and AP-2 {alpha}-appendage (blue) interaction motifs is indicated.