Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-D-aspartate receptors protects from calpain-mediated truncation of their C-terminaldomains
Autore:
Bi, RF; Rong, YQ; Bernard, A; Khrestchatisky, M; Baudry, M;
Indirizzi:
Univ So Calif, Program Neurosci, Los Angeles, CA 90089 USA Univ So Calif Los Angeles CA USA 90089 eurosci, Los Angeles, CA 90089 USA INSERM, U 29, INMED, F-13273 Marseille, France INSERM Marseille France F-13273 , U 29, INMED, F-13273 Marseille, France
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 34, volume: 275, anno: 2000,
pagine: 26477 - 26483
SICI:
0021-9258(20000825)275:34<26477:STPONS>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
NMDA-RECEPTOR; KINASE-C; BRAIN SPECTRIN; RAT-BRAIN; IN-VIVO; 2B; POTENTIATION; PROTEOLYSIS; NEURONS; PSD-95;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Baudry, M Univ So Calif, Program Neurosci, Los Angeles, CA 90089 USA Univ So Calif Los Angeles CA USA 90089 os Angeles, CA 90089 USA
Citazione:
R.F. Bi et al., "Src-mediated tyrosine phosphorylation of NR2 subunits of N-methyl-D-aspartate receptors protects from calpain-mediated truncation of their C-terminaldomains", J BIOL CHEM, 275(34), 2000, pp. 26477-26483

Abstract

Src-mediated tyrosine phosphorylation of N-methyl-D-aspartate receptor subunits has been shown to modify the functional properties of N-methyl-D-aspartate receptors. Moreover, calpain-mediated truncation of N-methyl-D-aspartate receptor subunits has been found to alter the structure of the receptors. In the present study, we first used immunoprecipitation with a variety of antibodies against N-methyl-D-aspartate receptor subunits and anti-phosphotyrosine antibodies to show that tyrosine-phosphorylated subunits of N-methyl-D-aspartate receptor are protected against calpain-mediated truncation of their C-terminal domains. A GST fusion protein containing the C-terminaldomain of NR2A was used to identify the calpain cutting sites in the C-terminal domain. One site was identified at residues 1278-1279, corresponding to one of the preferred calpain truncation sites. This site is adjacent to a consensus sequence for Src-mediated tyrosine phosphorylation, and Src mediated tyrosine phosphorylation of the GST-NR2A C-terminal fusion protein also inhibited calpain-mediated truncation of the fusion protein. We propose that phosphorylation of NR2 subunits and the resulting inhibition of calpain-mediated truncation of their C-terminal domains provide for the stabilization of the N-methyl-D-aspartate receptors in postsynaptic structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 10:00:10