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Titolo:
An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing
Autore:
Scott, DB; Blanpied, TA; Swanson, GT; Zhang, C; Ehlers, MD;
Indirizzi:
Duke Univ, Med Ctr, Dept Neurobiol, Durham, NC 27710 USA Duke Univ DurhamNC USA 27710 d Ctr, Dept Neurobiol, Durham, NC 27710 USA Duke Univ, Med Ctr, Cell & Mol Biol Program, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 ll & Mol Biol Program, Durham, NC 27710 USA Salk Inst Biol Studies, Mol Neurobiol Lab, La Jolla, CA 92037 USA Salk Inst Biol Studies La Jolla CA USA 92037 Lab, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 9, volume: 21, anno: 2001,
pagine: 3063 - 3072
SICI:
0270-6474(20010501)21:9<3063:ANRERS>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-SURFACE EXPRESSION; DENSITY PROTEIN PSD-95; C-TERMINAL DOMAIN; ENDOPLASMIC-RETICULUM; PLASMA-MEMBRANE; NR1 SUBUNIT; PDZ DOMAINS; ACETYLCHOLINE-RECEPTOR; SYNAPTIC LOCALIZATION; EXCITATORY SYNAPSES;
Keywords:
ER retention; NMDA receptors; NR1 subunit; RXR motif; quality control mechanisms; intracellular trafficking;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Ehlers, MD Duke Univ, Med Ctr, Dept Neurobiol, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 Neurobiol, Durham, NC 27710 USA
Citazione:
D.B. Scott et al., "An NMDA receptor ER retention signal regulated by phosphorylation and alternative splicing", J NEUROSC, 21(9), 2001, pp. 3063-3072

Abstract

Formation of mature excitatory synapses requires the assembly and deliveryof NMDA receptors to the neuronal plasma membrane. A key step in the trafficking of NMDA receptors to synapses is the exit of newly assembled receptors from the endoplasmic reticulum (ER). Here we report the identification of an RXR-type ER retention/retrieval motif in the C-terminal tail of the NMDA receptor subunit NR1 that regulates receptor surface expression in heterologous cells and in neurons. In addition, we show that PKC phosphorylationand an alternatively spliced consensus type I PDZ-binding domain suppress ER retention. These results demonstrate a novel quality control function for alternatively spliced C-terminal domains of NR1 and implicate both phosphorylation and potential PDZ-mediated interactions in the trafficking of NMDA receptors through early stages of the secretory pathway.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 13:20:57