Characterisation of the gene for Drosophila amphiphysin

• Published in: Gene 2000-01, Vol.241 (1), p.167-174
• Main Authors: Razzaq, Azam, Su, Ya, Mehren, Jennifer E., Mizuguchi, Kenji, Jackson, Antony P., Gay, Nicholas J., O'Kane, Cahir J.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; amino acid sequences; amphiphysin; animal proteins; Animals; binding proteins; Blotting, Southern; chromosome mapping; Clathrin; complementary DNA; DNA, Complementary - genetics; Drosophila; Drosophila - chemistry; Drosophila - embryology; Drosophila - genetics; Drosophila melanogaster; Dynamin; embryo (animal); embryogenesis; Endocytosis - genetics; endophilin; foregut; genbank/af171225; gene expression; genes; hindgut; In Situ Hybridization; integument; messenger RNA; Models, Molecular; molecular conformation; Molecular Sequence Data; Nerve Tissue Proteins - chemistry; Nerve Tissue Proteins - genetics; Nerve Tissue Proteins - metabolism; nucleic acid hybridization; nucleotide sequences; polytene chromosomes; Receptor-mediated endocytosis; Sequence Homology, Amino Acid; SH3 domain; src Homology Domains; Time Factors; Tissue Distribution
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/S0378-1119(99)00451-5

A sequence similarity search of the Drosophila nucleotide database using vertebrate amphiphysin as a query identified a cDNA that encodes a Drosophila amphiphysin. The predicted protein has conserved sequence domains that should enable it to dimerise and bind to dynamin. Structural modelling suggests that the Src-homology-3 (SH3) domains of vertebrate and Drosophila amphiphysins are highly similar, supporting the putative ability of the latter to bind dynamin. However, the fly amphiphysin shows less conservation to sequences in the vertebrate amphiphysins that bind other endocytic components such as clathrin, AP-2 and endophilin. Amphiphysin is a single-copy gene that maps to position 49B on polytene chromosomes. Messenger RNA of this amphiphysin is expressed widely during embryogenesis and has elevated expression in a number of sites including the foregut, hindgut and epidermis, but not in the central nervous system. Taken together, these data are consistent with a role for Drosophila amphiphysin in endocytosis, but the details of this role may differ from that of vertebrate amphiphysins.