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Phosphorylation of the carboxyl-terminal domain of the zeta 1 subunit is not responsible for potentiation by TPA of the NMDA receptor channel.

Abstract：

:The carboxyl-terminal domain of the zeta 1 subunit of the mouse NMDA receptor channel produced as a fusion protein with GST was phosphorylated in vitro by PKC. A mutant of the zeta 1 subunit without serine or threonine residues in the carboxyl-terminal domain (zeta 1-2-NST) was constructed and was expressed alone or together with the epsilon 2 subunit in Xenopus oocytes. Current responses of the zeta 1-2-NST homomeric and epsilon 2/zeta 1-2-NST heteromeric NMDA receptor channels were enhanced by treatment with TPA, a PKC activator, and the extents of potentiation were comparable with the corresponding wild-type channels. These results suggest that the phosphorylation of the carboxyl-terminal domain of the zeta 1 subunit is not responsible for potentiation of NMDA receptor channels by the TPA treatment.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Yamakura T,Mori H,Shimoji K,Mishina M

doi

10.1006/bbrc.1993.2426

subject

Has Abstract

pub_date

1993-11-15 00:00:00

pages

1537-44

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)72426-5

journal_volume

196

pub_type

杂志文章

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