Proteomics of Drosophila compound eyes: early studies, now, and the future--light-induced protein phosphorylation as an example.
In the past three decades, efforts to understand the molecular mechanisms underlying photoreceptor transduction of the fruit fly Drosophila melanogaster experienced drastic waves of technological development that involve multiple areas of scientific disciplines; the multidisciplinary approach includes a classical genetic manipulation in which random mutations are created and phenotypes are screened, a modern genetics maneuver in which a specific gene relevant to a hypothesis is molecularly cloned and manipulated, and, more recently, direct studies of proteins by proteomics technologies in combination with modern molecular biology and electrophysiology. This paper will review efforts that originated three decades ago in Professor William L. Pak's laboratory at Purdue University to study proteins involved in the Drosophila photoreceptor transduction process and show the power of such multidisciplinary approach that involves collaboration between molecular genetics, electrophysiology, and proteomics.
Department of Biochemistry and Molecular Biology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA. hiroyuki-matsumoto@ouhsc.edu
Hiroyuki
H
Matsumoto
D000818:Animals; D004330:Drosophila / Q000235:genetics* / Q000378:metabolism; D029721:Drosophila Proteins / Q000235:genetics* / Q000378:metabolism; D005123:Eye / Q000378:metabolism; D005136:Eye Proteins / Q000235:genetics* / Q000378:metabolism; D008027:Light; D009154:Mutation / Q000235:genetics; D010766:Phosphorylation / Q000187:drug effects / Q000235:genetics; D040901:Proteomics; D014785:Vision, Ocular / Q000235:genetics*
D029721:Drosophila Proteins; D005136:Eye Proteins; C520357:rtp protein, Drosophila