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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >MECHANISM OF RHODOPSIN PHOSPHORYLATION
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MECHANISM OF RHODOPSIN PHOSPHORYLATION

机译：视紫红质磷酸化的机理

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摘要

A key reaction in the inactivation of rhodopsin is its phosphorylation by rhodopsin kinase. In recent years, extensive studies related to rhodopsin kinase function and enzymatic properties were carried out. Rhodopsin kinase is a Ser/Thr protein kinase and a member of the G protein-coupled receptor kinases sub-family (GRKs) which consists of six recently identified members. Photolyzed rhodopsin is phosphorylated by rhodopsin kinase sequentially, with the first phosphate transferred preferentially to Ser-338, and subsequent phosphates transferred to Ser-343 and Thr-336. The binding of arrestin to the receptor, and reduction of the photolyzed chromophore all-trans-retinal to all-trans-retinol limits physiologically significant phosphorylation at no more than three sites (H. Ohguro, R.S. Johnson, L.H. Ericsson, K.A. Walsh and K. Palczewski, Biochemistry, 33 (1994) 1023). A similar phosphorylation reaction is implicated in most, if not all, G protein-coupled receptors during their desensitization. [References: 60]
机译：视紫红质灭活的关键反应是视紫红质激酶使其磷酸化。近年来，进行了关于视紫红质激酶功能和酶学性质的广泛研究。视紫红质激酶是一种Ser / Thr蛋白激酶，是G蛋白偶联受体激酶亚家族（GRKs）的成员，该家族由六个最近鉴定的成员组成。光解的视紫红质被视紫红质激酶依次磷酸化，其中第一种磷酸盐优先转移至Ser-338，随后的磷酸盐转移至Ser-343和Thr-336。抑制蛋白与受体的结合以及光解发色团的全反式视网膜向全反式视黄醇的还原限制了在不超过三个位点的生理上显着的磷酸化（H. Ohguro，RS Johnson，LH Ericsson，KA Walsh和K Palczewski，Biochemistry，33（1994）1023）。在大多数（如果不是全部）G蛋白偶联受体脱敏过程中，也会发生类似的磷酸化反应。 [参考：60]

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