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

被引：0
作者：
Daisuke Asai
Masaharu Murata
Riki Toita
Takahito Kawano
Hideki Nakashima
Jeong-Hun Kang
机构：
[1] St. Marianna University School of Medicine,Department of Microbiology
[2] Kyushu University,Department of Advanced Medical Initiatives, Faculty of Medical Sciences
[3] National Institute of Advanced Industrial Science and Technology (AIST),Biomedical Research Institute
[4] National Cerebral and Cardiovascular Center Research Institute,Division of Biopharmaceutics and Pharmacokinetics
来源：
Amino Acids | 2016年 / 48卷
关键词：
G protein-coupled receptor kinase; Amino acid residue; Phosphorylation; Cellular signal transduction pathway; Consensus sequence;
D O I：
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中图分类号：
学科分类号：
摘要：
A series of amino acid substitutions was made in a previously identified β-tubulin-derived GRK2 substrate peptide (404DEMEFTEAESNMN416) 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.
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页码：2875 / 2880
页数：5
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