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Published July 14, 1998 | public
Journal Article

Autophosphorylation and ADP Regulate the Ca^(2+)-Dependent Interaction of Recoverin with Rhodopsin Kinase


Recoverin is a 23 kDa myristoylated Ca^(2+)-binding protein that inhibits rhodopsin kinase. We have used surface plasmon resonance to investigate the influences of Ca^(2+), myristoylation, and adenine nucleotides on the recoverin−rhodopsin kinase interaction. Our analyses confirmed that Ca^(2+) is required for recoverin to bind RK. Myristoylation had little effect on the affinity of recoverin for the kinase, but it raised the K_(0.5) for Ca^(2+) from 150 nM for nonacylated recoverin to 400 nM for myristoylated recoverin. Finally, our studies also revealed two separate and previously unreported effects of adenine nucleotides on the recoverin−rhodopsin kinase binding. The interaction is weakened by autophosphorylation of the kinase, and it is strengthened by the presence of ADP.

Additional Information

© 1998 American Chemical Society. Received March 3, 1998; Revised Manuscript Received April 9, 1998; Publication Date (Web): June 18, 1998. This study was supported in part by grants from the Department of the Navy (96PRO7143-00) and from the American Heart Association Florida Affiliate, Inc. (Initial Investigator Award 9603008) to V.Z.S. and from the National Eye Institute (EY06641) to J.B.H. D.K.S. was supported by the American Heart Association Florida Affiliate, Inc., Postdoctoral Fellowship 9703012. We thank Dr. E. Lee (University of Miami) for providing protein phosphatase PP1.

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October 18, 2023