A single amino acid residue determines the Ca2+ permeability of AMPA-selective glutamate receptor channels

Masayoshi Mishina; Kenji Sakimura; Hisashi Mori; Etsuko Kushiya; Masayuki Harabayashi; Shigeo Uchino; Kenji Nagahari

doi:10.1016/S0006-291X(05)81137-4

A single amino acid residue determines the Ca²⁺ permeability of AMPA-selective glutamate receptor channels

Masayoshi Mishina^*, Kenji Sakimura, Hisashi Mori, Etsuko Kushiya, Masayuki Harabayashi, Shigeo Uchino, Kenji Nagahari

^*Corresponding author for this work

Molecular Neuroscience

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

69 Scopus citations

Abstract

Functional analysis of AMPA-selective glutamate receptor channels expressed in Xenopus oocytes from cloned cDNAs has shown that homomeric channels formed by the G1uR1 subunit are permeable to Ca²⁺, whereas heteromeric channels composed of the GluR1 and G1uR2 subunits show little permeability. Furthermore, substitution of glutamine for arginine in putative transmembrane segment M2 of the GluR2 subunit makes the heteromeric channels permeable to Ca²⁺. These results suggest that the G1uR2 subunit plays a key role in keeping AMPAselective glutamate receptor channels essentially impermeable to Ca²⁺ and that the critical determinant is the positively charged residue in M2 segment.

Original language	English
Pages (from-to)	813-821
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	180
Issue number	2
DOIs	https://doi.org/10.1016/S0006-291X(05)81137-4
State	Published - 1991/10/31

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/S0006-291X(05)81137-4

Cite this

@article{8e0770dd347b4719a574b54dc9684ec3,

title = "A single amino acid residue determines the Ca2+ permeability of AMPA-selective glutamate receptor channels",

abstract = "Functional analysis of AMPA-selective glutamate receptor channels expressed in Xenopus oocytes from cloned cDNAs has shown that homomeric channels formed by the G1uR1 subunit are permeable to Ca2+, whereas heteromeric channels composed of the GluR1 and G1uR2 subunits show little permeability. Furthermore, substitution of glutamine for arginine in putative transmembrane segment M2 of the GluR2 subunit makes the heteromeric channels permeable to Ca2+. These results suggest that the G1uR2 subunit plays a key role in keeping AMPAselective glutamate receptor channels essentially impermeable to Ca2+ and that the critical determinant is the positively charged residue in M2 segment.",

author = "Masayoshi Mishina and Kenji Sakimura and Hisashi Mori and Etsuko Kushiya and Masayuki Harabayashi and Shigeo Uchino and Kenji Nagahari",

note = "Funding Information: We thank Miss Mutsuko Motokoshi for her invaluable assistance. This investigation was supported in part by research grants from the Ministry of Education, Science and Culture of Japan, the Institute of Physical and Chemical Research, the Ministry of Health and Welfare of Japan, the Naito Foundation (M. M.) and the New Energy and Industrial Technology Development Organization (K. N.).",

year = "1991",

month = oct,

day = "31",

doi = "10.1016/S0006-291X(05)81137-4",

language = "英語",

volume = "180",

pages = "813--821",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier B.V.",

number = "2",

}

TY - JOUR

T1 - A single amino acid residue determines the Ca2+ permeability of AMPA-selective glutamate receptor channels

AU - Mishina, Masayoshi

AU - Sakimura, Kenji

AU - Mori, Hisashi

AU - Kushiya, Etsuko

AU - Harabayashi, Masayuki

AU - Uchino, Shigeo

AU - Nagahari, Kenji

N1 - Funding Information: We thank Miss Mutsuko Motokoshi for her invaluable assistance. This investigation was supported in part by research grants from the Ministry of Education, Science and Culture of Japan, the Institute of Physical and Chemical Research, the Ministry of Health and Welfare of Japan, the Naito Foundation (M. M.) and the New Energy and Industrial Technology Development Organization (K. N.).

PY - 1991/10/31

Y1 - 1991/10/31

N2 - Functional analysis of AMPA-selective glutamate receptor channels expressed in Xenopus oocytes from cloned cDNAs has shown that homomeric channels formed by the G1uR1 subunit are permeable to Ca2+, whereas heteromeric channels composed of the GluR1 and G1uR2 subunits show little permeability. Furthermore, substitution of glutamine for arginine in putative transmembrane segment M2 of the GluR2 subunit makes the heteromeric channels permeable to Ca2+. These results suggest that the G1uR2 subunit plays a key role in keeping AMPAselective glutamate receptor channels essentially impermeable to Ca2+ and that the critical determinant is the positively charged residue in M2 segment.

AB - Functional analysis of AMPA-selective glutamate receptor channels expressed in Xenopus oocytes from cloned cDNAs has shown that homomeric channels formed by the G1uR1 subunit are permeable to Ca2+, whereas heteromeric channels composed of the GluR1 and G1uR2 subunits show little permeability. Furthermore, substitution of glutamine for arginine in putative transmembrane segment M2 of the GluR2 subunit makes the heteromeric channels permeable to Ca2+. These results suggest that the G1uR2 subunit plays a key role in keeping AMPAselective glutamate receptor channels essentially impermeable to Ca2+ and that the critical determinant is the positively charged residue in M2 segment.

UR - http://www.scopus.com/inward/record.url?scp=0025718815&partnerID=8YFLogxK

U2 - 10.1016/S0006-291X(05)81137-4

DO - 10.1016/S0006-291X(05)81137-4

M3 - 学術論文

C2 - 1659403

AN - SCOPUS:0025718815

SN - 0006-291X

VL - 180

SP - 813

EP - 821

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2