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Titolo:
Opposing changes in phosphorylation of specific sites in synapsin I duringCa2+-dependent glutamate release in isolated nerve terminals
Autore:
Jovanovic, JN; Sihra, TS; Nairn, AC; Hemmings, HC; Greengard, P; Czernik, AJ;
Indirizzi:
Univ Coll London, Dept Pharmacol, London WC1E 6BT, England Univ Coll London London England WC1E 6BT macol, London WC1E 6BT, England Rockefeller Univ, Mol & Cellular Neurosci Lab, New York, NY 10021 USA Rockefeller Univ New York NY USA 10021 urosci Lab, New York, NY 10021 USA Cornell Univ, Weill Med Coll, Dept Anesthesiol, New York, NY 10021 USA Cornell Univ New York NY USA 10021 pt Anesthesiol, New York, NY 10021 USA Cornell Univ, Weill Med Coll, Dept Pharmacol, New York, NY 10021 USA Cornell Univ New York NY USA 10021 Dept Pharmacol, New York, NY 10021 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 20, volume: 21, anno: 2001,
pagine: 7944 - 7953
SICI:
0270-6474(20011015)21:20<7944:OCIPOS>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT PROTEIN-KINASE; SMALL SYNAPTIC VESICLES; RABBIT SKELETAL-MUSCLE; NEUROTRANSMITTER RELEASE; CYCLIC-AMP; NEUROMUSCULAR-JUNCTION; CATALYTIC SUBUNIT; MAMMALIAN BRAIN; PHOSPHATASE 2A; RAT FOREBRAIN;
Keywords:
4-aminopyridine; brain-derived neurotrophic factor (BDNF); Ca2+; calcineurin; cyclosporin A; glutamate; ionomycin; mitogen-activated protein (MAP) kinase; neurotrophins; okadaic acid; PD98059; phosphatases; synapsins; synaptosomes; neurotransmitter release;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Jovanovic, JN Univ Coll London, Dept Pharmacol, Mortimer St, London WC1E 6BT, England Univ Coll London Mortimer St London England WC1E 6BT ngland
Citazione:
J.N. Jovanovic et al., "Opposing changes in phosphorylation of specific sites in synapsin I duringCa2+-dependent glutamate release in isolated nerve terminals", J NEUROSC, 21(20), 2001, pp. 7944-7953

Abstract

Synapsins are major neuronal phosphoproteins involved in regulation of neurotransmitter release. Synapsins are well established targets for multiple protein kinases within the nerve terminal, yet little is known about dephosphorylation processes involved in regulation of synapsin function. Here, weobserved a reciprocal relationship in the phosphorylation-dephosphorylation of the established phosphorylation sites on synapsin I. We demonstrate that, in vitro, phosphorylation sites 1, 2, and 3 of synapsin I (P-site 1 phosphorylated by cAMP-dependent protein kinase; P-sites 2 and 3 phosphorylated by Ca2+ calmodulin-dependent protein kinase II) were excellent substratesfor protein phosphatase 2A, whereas P-sites 4, 5, and 6 (phosphorylated bymitogen-activated protein kinase) were efficiently dephosphorylated only by Ca2+-calmodulin-dependent protein phosphatase 2B-calcineurin. In isolatednerve terminals, rapid changes in synapsin I phosphorylation were observedafter Ca2+ entry, namely, a Ca2+-dependent phosphorylation of P-sites 1, 2, and 3 and a Ca2+-dependent dephosphorylation of P-sites 4, 5, and 6. Inhibition of calcineurin activity by cyclosporin A resulted in a complete block of Ca2+-dependent dephosphorylation of P-sites 4, 5, and 6 and correlatedwith a prominent increase in ionomycin-evoked glutamate release. These twoopposing, rapid, Ca2+-dependent processes may play a crucial role in the modulation of synaptic vesicle trafficking within the presynaptic terminal.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 02:58:13