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- W2014000003 abstract "Bovine recoverin regulates rhodopsin phosphorylation and controls photoreceptor light sensitivity in a Ca(2+)-dependent manner. Recoverin is post-translationally modified with lipids (myristic acid or related lipids) at its N-terminus. Since with this lipid modification (N-myristoylation), recoverin associates with rod outer segment membranes in a Ca(2+)-dependent manner, N-myristoylation has been suggested to be important for the function of this protein. To study the role of this modification, we obtained recombinant non-myristoylated recoverin in E. coli and studied its functional properties. Here, we report that recombinant non-myristoylated recoverin inhibits rhodopsin phosphorylation at Ca2+ concentrations of 30 nM-10 microM in a similar way as native N-myristoylated recoverin does. Thus, our result showed that N-myristoylation is not essential for the Ca(2+)-dependent inhibition of rhodopsin phosphorylation by recoverin." @default.
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- W2014000003 date "1994-08-01" @default.
- W2014000003 modified "2023-09-23" @default.
- W2014000003 title "Inhibition of Rhodopsin Phosphorylation by Non-Myristoylated Recombinant Recoverin" @default.
- W2014000003 doi "https://doi.org/10.1006/bbrc.1994.2157" @default.
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