Cloning and expression of the epsilon 4 subunit of the NMDA receptor channel.
The primary structure of a novel subunit of the mouse NMDA (N-methyl-D-aspartate) receptor channel, designated epsilon 4, has been revealed by cloning and sequencing the cDNA. The epsilon 4 subunit shares high amino acid sequence identity with the epsilon 1, epsilon 2 and epsilon 3 subunits of the mouse NMDA receptor channel, thus constituting the epsilon subfamily of the glutamate receptor channel. Expression from cloned cDNAs of the epsilon 4 subunit together with the zeta 1 subunit in Xenopus oocytes yields functional NMDA receptor channels. The epsilon 4/zeta 1 heteromeric channel exhibits high apparent affinities for agonists and low sensitivities to competitive antagonists. The epsilon 4 subunit is thus distinct in functional properties from the epsilon 1, epsilon 2 and epsilon 3 subunits, and contributes further diversity of the NMDA receptor channel.
Ikeda
K
K
Department of Neuropharmacology, Niigata University, Japan.
Nagasawa
M
M
Mori
H
H
Araki
K
K
Sakimura
K
K
Watanabe
M
M
Inoue
Y
Y
Mishina
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA; D015870:Gene Expression; D007473:Ion Channels / Q000235:genetics*; D008564:Membrane Potentials; D051379:Mice; D008969:Molecular Sequence Data; D016194:Receptors, N-Methyl-D-Aspartate / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D014982:Xenopus laevis
D007473:Ion Channels; D016194:Receptors, N-Methyl-D-Aspartate; D004247:DNA