Autophosphorylation and ADP regulate the Ca2+-dependent interaction of recoverin with rhodopsin kinase

Daulet K. Satpaev, Ching Kang Chen, Anthony Scotti, Melvin I. Simon, James B. Hurley, Vladlen Z. Slepak

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Recoverin is a 23 kDa myristoylated Ca2+-binding protein that inhibits rhodopsin kinase. We have used surface plasmon resonance to investigate the influences of Ca2+, myristoylation, and adenine nucleotides on the recoverin-rhodopsin kinase interaction. Our analyses confirmed that Ca2+ is required for recoverin to bind RK. Myristoylation had little effect on the affinity of recoverin for the kinase, but it raised the K0.5 for Ca2+ 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.

Original languageEnglish (US)
Pages (from-to)10256-10262
Number of pages7
JournalBiochemistry
Volume37
Issue number28
DOIs
StatePublished - Jul 14 1998

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'Autophosphorylation and ADP regulate the Ca<sup>2+</sup>-dependent interaction of recoverin with rhodopsin kinase'. Together they form a unique fingerprint.

  • Cite this