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O ‐Glycosylation of G‐protein‐coupled receptor, octopus rhodopsin
Author(s) -
Nakagawa Masashi,
Miyamoto Takayuki,
Kusakabe Rie,
Takasaki Seiichi,
Takao Toshifumi,
Shichida Yoshinori,
Tsuda Motoyuki
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02392-4
Subject(s) - rhodopsin , octopus (software) , g protein coupled receptor , glycan , glycosylation , chemistry , biochemistry , receptor , edman degradation , biology , peptide sequence , glycoprotein , retinal , computational chemistry , gene
In addition to the N ‐glycan that is evidently conserved in G‐protein‐coupled receptors (GPCRs), O ‐glycans in the N‐terminus of GPCRs have been suggested. Using a combination of enzymatic and manual Edman degradation in conjunction with G‐protein coupled receptor mass spectrometry, the structure and sites of O ‐glycans in octopus rhodopsin are determined. Two N ‐acetylgalactosamine residues are O ‐linked to Thr4 and Thr5 in the N‐terminus of octopus rhodopsin. Further, we found chicken iodopsin, but not bovine rhodopsin, contains N ‐acetylgalactosamine. This is the first direct evidence to determine the structure and sites of O ‐glycans in GPCRs.