One of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase

Komolov, K. E.; Senin, I. I.; Weiergräber, Oliver H.; Koch, K. W.; Vaganova, S. A.; Philippov, P. P.; Churumova, V. A.; Zinchenko, D. V.

Journal Article

FZJ-2013-03329

One of the Ca(2+) binding sites of recoverin exclusively controls interaction with rhodopsin kinase

Komolov, K. E. (Corresponding author) ; Zinchenko, D. V. ; Churumova, V. A. ; Vaganova, S. A. ; Weiergräber, O. H.FZJ* ; Senin, I. I. ; Philippov, P. P. ; Koch, K. W.

2005
de Gruyter Berlin [u.a.]

Biological chemistry 386, 285-286 (2005) [10.1515/BC.2005.034]

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Please use a persistent id in citations: http://hdl.handle.net/2128/18397 doi:10.1515/BC.2005.034

Abstract: Recoverin is a neuronal calcium sensor protein that controls the activity of rhodopsin kinase in a Ca(2+)-dependent manner. Mutations in the EF-hand Ca2+ binding sites are valuable tools for investigating the functional properties of recoverin. In the recoverin mutant E121Q (Rec E121Q ) the high-affinity Ca2+ binding site is disabled. The non-myristoylated form of Rec E121Q binds one Ca2+ via its second Ca(2+)-binding site (EF-hand 2), whereas the myristoylated variant does not bind Ca2+ at all. Binding of Ca2+ to non-myristoylated Rec E121Q apparently triggers exposure of apolar side chains, allowing for association with hydrophobic matrices. Likewise, an interaction surface for the recoverin target rhodopsin kinase is constituted upon Ca2+ binding to the non-acylated mutant. Structural changes resulting from Ca(2+)-occupation of EF-hand 2 in myristoylated and non-myristoylated recoverin variants are discussed in terms of critical conditions required for biological activity.

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