Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

被引：4
|
作者：
Asai, Daisuke [1 ]
Murata, Masaharu [2 ]
Toita, Riki [3 ]
Kawano, Takahito [2 ]
Nakashima, Hideki [1 ]
Kang, Jeong-Hun [4 ]
机构：
[1] St Marianna Univ, Sch Med, Dept Microbiol, Sugao 2-16-1 Miyamae, Kawasaki, Kanagawa 2168511, Japan
[2] Kyushu Univ, Fac Med Sci, Dept Adv Med Initiat, Higashi Ku, 3-1-1 Maidashi, Fukuoka 8128582, Japan
[3] Natl Inst Adv Ind Sci & Technol, Biomed Res Inst, 1-8-31 Midorioka, Ikeda, Osaka 5638577, Japan
[4] Natl Cerebral & Cardiovasc Ctr, Res Inst, Div Biopharmaceut & Pharmacokinet, 5-7-1 Fujishiro Dai, Suita, Osaka 5658565, Japan
来源：
AMINO ACIDS | 2016年 / 48卷 / 12期
关键词：
G protein-coupled receptor kinase; Amino acid residue; Phosphorylation; Cellular signal transduction pathway; Consensus sequence; BETA; IDENTIFICATION; TRAFFICKING; ANTAGONIST; UNVEILS; TUBULIN;
D O I：
10.1007/s00726-016-2345-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A series of amino acid substitutions was made in a previously identified beta-tubulin-derived GRK2 substrate peptide ((404)DEMEFTEAESNMN(416)) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.
引用
收藏
页码：2875 / 2880
页数：6
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