Date of Award

Winter 2010

Project Type

Thesis

Program or Major

Biochemistry and Molecular Biology

Degree Name

Master of Science

First Advisor

Richard H Cote

Abstract

Photoreceptor phosphodiesterase (PDE6) is a central component of the visual pathway. While initial PDE6 activation following light stimulation of photoreceptors is well understood, regulation of PDE6 during recovery and light adaptation may require additional components that interact with PDE6. Two approaches were taken to characterize these potential interactions. The first explored the interaction of PDE6 with prenyl binding protein (PrBP/delta) and demonstrated that changes in membrane localization of PDE6 may occur during light adaptation as a result of association with PrBP/delta. The second approach characterized the PDE6 "interactome" by a mass spectrometric identification of 75 proteins that co-purify with PDE6 upon release from photoreceptor membranes. This work advances our understanding of the role of PrBP/delta in photoreceptors and provides an initial characterization of the entire complement of PDE6 binding partners in photoreceptors.

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