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Titolo:
Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex
Autore:
Chheda, MG; Ashery, U; Thakur, P; Rettig, J; Sheng, ZH;
Indirizzi:
Natl Inst Neurol Disorders & Stroke, Synapt Funct Unit, NIH, Bethesda, MD 20892 USA Natl Inst Neurol Disorders & Stroke Bethesda MD USA 20892 a, MD 20892 USA Max Planck Inst Biophys Chem, Dept Membrane Biophys, D-37077 Gottingen, Germany Max Planck Inst Biophys Chem Gottingen Germany D-37077 ottingen, Germany
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 4, volume: 3, anno: 2001,
pagine: 331 - 338
SICI:
1465-7392(200104)3:4<331:POSBPM>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
LONG-TERM POTENTIATION; PROTEIN-PROTEIN INTERACTIONS; NEUROTRANSMITTER RELEASE; SYNAPTIC TRANSMISSION; TRANSMITTER RELEASE; MEMBRANE-FUSION; HIPPOCAMPAL-NEURONS; SECRETORY MACHINERY; CHROMAFFIN CELLS; CALCIUM CHANNELS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Sheng, ZH Natl Inst Neurol Disorders & Stroke, Synapt Funct Unit, NIH, 36 Convent Dr, Bethesda, MD 20892 USA Natl Inst Neurol Disorders & Stroke 36 Convent Dr Bethesda MD USA 20892
Citazione:
M.G. Chheda et al., "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex", NAT CELL BI, 3(4), 2001, pp. 331-338

Abstract

cAMP-dependent protein kinase A (PKA) can modulate synaptic transmission by acting directly on unknown targets in the neurotransmitter secretory machinery. Here we identify Snapin, a protein of relative molecular mass 15,000that is implicated in neurotransmission by binding to SNAP-25, as a possible target. Deletion mutation and site-directed mutagenetic experiments pinpoint the phosphorylation site to serine 50. PKA-phosphorylation of Snapin significantly increases its binding to synaptosomal-associated protein-25 (SNAP-25). Mutation of Snapin serine 50 to aspartic acid (S50D) mimics this effect of PKA phosphorylation and enhances the association of synaptotagmin with the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex. Furthermore, treatment of rat hippocampal slices with nonhydrolysable cAMP analogue induces in vivo phosphorylation of Snapin andenhances the interaction of both Snapin and synaptotagmin with the SNARE complex. In adrenal chromaffin cells, overexpression of the Snapin S50D mutant leads to an increase in the number of release-competent vesicles. Our results indicate that Snapin may be a PKA target for modulating transmitter release through the cAMP-dependent signal-transduction pathway.

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Documento generato il 21/01/20 alle ore 06:59:34