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Titolo:
Protein kinase C potentiation of N-methyl-D-aspartate receptor activity isnot mediated by phosphorylation of N-methyl-D-aspartate receptor subunits
Autore:
Zheng, X; Zhang, L; Wang, AP; Bennett, MVL; Zukin, RS;
Indirizzi:
Yeshiva Univ Albert Einstein Coll Med, Dept Neurosci, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 26, volume: 96, anno: 1999,
pagine: 15262 - 15267
SICI:
0027-8424(199912)96:26<15262:PKCPON>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECOMBINANT NMDA RECEPTORS; SPLICE VARIANTS; XENOPUS OOCYTES; RAT-BRAIN; GLUTAMATE RECEPTORS; MESSENGER-RNA; NR1 SUBUNIT; RESPONSES; MODULATION; POLYAMINES;
Keywords:
excitatory amino acids; site-directed mutagenesis;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Bennett, MVL Yeshiva Univ Albert Einstein Coll Med, Dept Neurosci, 1300 Morris Pk Ave, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med 1300Morris Pk Ave Bronx NY USA 10461
Citazione:
X. Zheng et al., "Protein kinase C potentiation of N-methyl-D-aspartate receptor activity isnot mediated by phosphorylation of N-methyl-D-aspartate receptor subunits", P NAS US, 96(26), 1999, pp. 15262-15267

Abstract

N-methyl-D-aspartate receptors (NMDARs) are Ca2+-permeable glutamate-gatedion channels whose physiological properties in neurons are modulated by protein kinase C (PKC). The present study was undertaken to determine the role in PKC-induced potentiation of the NR1 and NR2A C-terminal tails, which serve as targets of PKC phosphorylation [Tingley, W. G., Ehlers, M. D., Kameyama, K., Doherty, C., Ptak, J. B., Riley, C. T. & Huganir, R. L. (1997) J. Biol. Chem. 272, 5157-5166]. Serine residue 890 in the C1 cassette is a primary target of PKC phosphorylation and a critical residue in receptor clustering at the membrane. We report herein that the presence of the C1 cassette reduces PKC potentiation and that mutation of Ser-890 significantly restores PKC potentiation. Splicing out or deletion of other C-terminal cassettes singly or in combination had little or no effect on PKC potentiation. Moreover, experiments involving truncation mutants reveal the unexpected finding that NMDARs assembled from subunits lacking all known sites of PKC phosphorylation can show PKC potentiation. These results indicate that PKC-induced potentiation of NMDAR activity does not occur by direct phosphorylationof the receptor protein but rather of associated targeting, anchoring, or signaling protein(s). PKC potentiation of NMDAR function is likely to be animportant mode of NMDAR regulation in vivo and may play a role in NMDA-dependent long-term potentiation.

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Documento generato il 11/07/20 alle ore 20:28:06