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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Autophosphorylation and ADP regulate the Ca2+-dependent interaction of recoverin with rhodopsin kinase. Satpaev, D.K., Chen, C.K., Scotti, A., Simon, M.I., Hurley, J.B., Slepak, V.Z. Biochemistry (1998) [Pubmed]
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