High levels of rhodopsin phosphorylation in missense mutations of C‐terminal region of rhodopsin

FEBS Letters

Ohguro, Hiroshi¹ 

[1] Department of Ophthalmology, Sapporo Medical University, School of Medicine, S-1 W-16, Chuo-ku, Sapporo 060, Japan

关键词: Rhodopsin phosphorylation;    Rhodopsin;    Rhodopsin kinase;    Retinitis pigmentosa;   

DOI  :  10.1016/S0014-5793(97)00957-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Rhodopsin phosphorylation was investigated using synthetic C-terminal peptides from rhodopsin. The peptides were phosphorylated by expressed rhodopsin kinase (RK) in the presence of a photolyzed truncated rhodopsin at the C-terminus. No peptide phosphorylation was detected under dark or in conditions in which RK was inactive. However, the phosphorylation rate was significantly higher in the following three peptides: (345M Rho, 330DDEASTTVSKTETSQMAPA; 347S Rho, 330DDEASTTVSKTETSQVASA; and 347L Rho: 330DDEASTTVSKTETSQVALA) taken from missense mutations of rhodopsin found in patients with autosomal retinitis pigmentosa (ADRP) as compared with that from wild-type rhodopsin (330DDEASTTVSKTETSQVAPA). Distribution of the phosphorylation showed a similar ratio among three serines (334, 338 and 343) in 347L Rho mutation to wild type. However, 345M Rho and 347S Rho peptides showed higher phosphorylation at Ser³³⁴. The data obtained suggests that an abnormally high rate of phosphorylation in missense mutations around the rhodopsin C-terminus may change the position of phosphorylation and inactivation process of the visual transduction.

【 授权许可】

Unknown