Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)
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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.
KeywordsG protein-coupled receptor kinase Amino acid residue Phosphorylation Cellular signal transduction pathway Consensus sequence
The authors thank Ms. Sigemi Terakubo and Ms. Niño Okamura (St. Marianna University School of Medicine) for technical assistance. This work was supported by a Grant-in-Aid for Challenging Exploratory Research (KAKENHI Grant Number 15K12531) and for Scientific Research (C) (15K01319) from the Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan.
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Conflict of interest
The authors declare that they have no conflict of interest.
This article does not contain any studies with human participants or animals performed by any of the authors.
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