Proteomics of Drosophila Compound Eyes: Early Studies, Now, and the Future—Light-Induced Protein Phosphorylation as an Example

Abstract:

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.

Keywords::

• 2-D gels
• Drosophila compound eyes
• mass spectrometry
• protein maps
• protein phosphorylation
• proteomics
• reverse genetics

ACKNOWLEDGMENTS

The development of this project in the Matsumoto laboratory at the University of Oklahoma Health Sciences Center has been supported by grants from NSF (BNS 83 15599 and BNS 83 11203) and from NIH (EY06595 and EY13877) in the past 30 years. I also acknowledge all my colleagues who participated in the project described in this review.

Declaration of interest: The author reports no conflicts of interest. The author alone is responsible for the content and writing of the paper.