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

Daisuke Asai; Masaharu Murata; Riki Toita; Takahito Kawano; Hideki Nakashima; Jeong Hun Kang

doi:10.1007/s00726-016-2345-6

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

Daisuke Asai, Masaharu Murata, Riki Toita, Takahito Kawano, Hideki Nakashima, Jeong Hun Kang

Center for Advanced Medical Open Innovation

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	2875-2880
Number of pages	6
Journal	Amino Acids
Volume	48
Issue number	12
DOIs	https://doi.org/10.1007/s00726-016-2345-6
Publication status	Published - Dec 1 2016

All Science Journal Classification (ASJC) codes

Biochemistry
Clinical Biochemistry
Organic Chemistry

Access to Document

10.1007/s00726-016-2345-6

Cite this

@article{2562579d455145cba08908a6bd6c381e,

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

abstract = "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.",

author = "Daisuke Asai and Masaharu Murata and Riki Toita and Takahito Kawano and Hideki Nakashima and Kang, {Jeong Hun}",

note = "Funding Information: The authors thank Ms. Sigemi Terakubo and Ms. Ni{\~n}o 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. Publisher Copyright: {\textcopyright} 2016, Springer-Verlag Wien.",

year = "2016",

month = dec,

day = "1",

doi = "10.1007/s00726-016-2345-6",

language = "English",

volume = "48",

pages = "2875--2880",

journal = "Amino Acids",

issn = "0939-4451",

publisher = "Springer Wien",

number = "12",

}

TY - JOUR

T1 - Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2)

AU - Asai, Daisuke

AU - Murata, Masaharu

AU - Toita, Riki

AU - Kawano, Takahito

AU - Nakashima, Hideki

AU - Kang, Jeong Hun

N1 - Funding Information: 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. Publisher Copyright: © 2016, Springer-Verlag Wien.

PY - 2016/12/1

Y1 - 2016/12/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84990978754&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84990978754&partnerID=8YFLogxK

U2 - 10.1007/s00726-016-2345-6

DO - 10.1007/s00726-016-2345-6

M3 - Article

C2 - 27714516

AN - SCOPUS:84990978754

VL - 48

SP - 2875

EP - 2880

JO - Amino Acids

JF - Amino Acids

SN - 0939-4451

IS - 12

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this