Light-mediated signal transduction in vertebrate retina involves the absorption of light by the chromophore of the visual pigment rhodopsin. Absorption of a photon leads to the isomerization of the chromophore, formation of activated rhodopsin, and subsequent phosphorylation of rhodopsin by rhodopsin kinase. Arrestin preferentially binds light- activated, phosphorylated rhodopsin rather than nonphosphorylated rhodopsin, thus quenching light-mediated signal transduction. It is hypothesis using recombinant arrestin constructs in which the two positively charged domains are either eliminated, substituted with negatively charged amino acids, or substituted with neutral amino acids. These constructs will be expressed in a heterologous system and the binding of these expressed arrestin proteins to phosphorylated rhodopsin will be compared to that of native arrestin.

Agency
National Institute of Health (NIH)
Institute
National Eye Institute (NEI)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32EY006641-01
Application #
2160694
Study Section
Visual Sciences C Study Section (VISC)
Project Start
1995-08-15
Project End
Budget Start
1995-02-15
Budget End
1996-02-14
Support Year
1
Fiscal Year
1995
Total Cost
Indirect Cost
Name
University of Florida
Department
Ophthalmology
Type
Schools of Medicine
DUNS #
073130411
City
Gainesville
State
FL
Country
United States
Zip Code
32611
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