Details

Autor(en) / Beteiligte

• Kawamura, S.
• Cox, J.A.
• Nef, P.

Titel

Inhibition of Rhodopsin Phosphorylation by Non-Myristoylated Recombinant Recoverin

Ist Teil von

• Biochemical and biophysical research communications, 1994-08, Vol.203 (1), p.121-127

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

1994

Quelle

Elsevier Journal Backfiles on ScienceDirect (DFG Nationallizenzen)

Beschreibungen/Notizen

• Bovine recoverin regulates rhodopsin phosphorylation and controls photoreceptor light sensitivity in a Ca2+-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 Ca2+-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 μM in a similar way as native N-myristoylated recoverin does. Thus, our result showed that N-myristoylation is not essential for the Ca2+-dependent inhibition of rhodopsin phosphorylation by recoverin.