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Identification of a Single Phosphorylation Site Within Octopus Rhodopsin
Author(s) -
Ohguro Hiroshi,
Yoshida Norihiko,
Shindou Hideo,
Crabb John W.,
Palczewski Krzysztof,
Tsuda Motoyuki
Publication year - 1998
Publication title -
photochemistry and photobiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.818
H-Index - 131
eISSN - 1751-1097
pISSN - 0031-8655
DOI - 10.1111/j.1751-1097.1998.tb05290.x
Subject(s) - rhodopsin , phosphorylation , octopus (software) , visual phototransduction , signal transduction , biology , kinase , microbiology and biotechnology , arrestin , protein phosphorylation , g protein coupled receptor , chemistry , biochemistry , protein kinase a , retinal , computational chemistry
— Light‐dependent phosphorylation of rhodopsin (Rho) is a first step in the desensitization of the signaling state of the receptor during vertebrate and invertebrate visual transduction. We found that only 358 Ser of the photoac‐tivated octopus Rho (oRho*) was phosphorylated by octopus rhodopsin kinase (oRK). Tryptic truncation of the C‐terminal PPQGY repeats of oRho that follow the phosphorylation region did not influence spectral or G‐protein activation properties of oRho but abolished phos phorylation. Despite significant structural differences between oRK and mammalian RK, these results provide i further evidence of the importance of singly phosphorylated species of Rho* in the generation of arrestin binding sites.