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Titolo:
Stages of synapse development defined by dependence on F-actin
Autore:
Zhang, WD; Benson, DL;
Indirizzi:
CUNY Mt Sinai Sch Med, Fishberg Res Ctr Neurobiol, New York, NY 10029 USA CUNY Mt Sinai Sch Med New York NY USA 10029 obiol, New York, NY 10029 USA CUNY Mt Sinai Sch Med, Program Cell Adhes, New York, NY 10029 USA CUNY Mt Sinai Sch Med New York NY USA 10029 Adhes, New York, NY 10029 USA
Titolo Testata:
JOURNAL OF NEUROSCIENCE
fascicolo: 14, volume: 21, anno: 2001,
pagine: 5169 - 5181
SICI:
0270-6474(20010715)21:14<5169:SOSDDB>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HIPPOCAMPAL-NEURONS; HEPARAN-SULFATE PROTEOGLYCAN; SINGLE PRESYNAPTIC BOUTONS; LONG-TERM POTENTIATION; CELL-CELL ADHESION; DENDRITIC SPINES; NEUROTRANSMITTER RELEASE; N-CADHERIN; NEUROMUSCULAR-JUNCTIONS; RECEPTOR ACTIVATION;
Keywords:
actin; presynaptic terminal; postsynaptic density; Bassoon; synaptophysin; tetanus toxin; PSD-95; cadherin; synapse adhesion; alpha-internexin; dendritic spines;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
95
Recensione:
Indirizzi per estratti:
Indirizzo: Benson, DL CUNY Mt Sinai Sch Med, Fishberg Res Ctr Neurobiol, Box 1065,1425 Madison Ave, New York, NY 10029 USA CUNY Mt Sinai Sch Med Box 1065,1425 Madison Ave New York NY USA 10029
Citazione:
W.D. Zhang e D.L. Benson, "Stages of synapse development defined by dependence on F-actin", J NEUROSC, 21(14), 2001, pp. 5169-5181

Abstract

It has been widely speculated that actin plays a central role in CNS synapse assembly, but such a requirement for actin filaments (F-actin) has not yet been demonstrated experimentally. We used hippocampal neurons grown in culture and the actin depolymerizing agent, latrunculin A, to examine directly the relationship between F-actin and synapse formation and maturation. During the first week in culture, actin depolymerization results in a near complete loss of synapses defined by synaptophysin-labeled vesicle clusters,synaptic vesicle recycling, and ultrastructure. Over the second week in culture, F-actin becomes increasingly stable, but actin depolymerization no longer disrupts basic synaptic structure. There is, however, a reduction in the number and size of synaptophysin-labeled clusters and in the size of vesicle clusters undergoing FM4-64 recycling, suggesting that synaptic vesicle anchoring remains partially dependent on F-actin. By 18 d in culture, synaptophysin clusters and synaptic vesicle recycling are largely resistant toF-actin depolymerization. The decrease in synapse dependence on F-actin correlates well with the acquisition and retention of presynaptic scaffoldingproteins such as Bassoon and postsynaptic scaffolding proteins such as those of the postsynaptic density-95 family. Increased activity stabilizes F-actin and its associated proteins at synaptic sites, suggesting a correlation between active synapses, actin stability, and synapse stability. Our findings demonstrate that F-actin is essential for the development and maintenance of young synapses. Because F-actin is also highly regulatable, we propose that F-actin may be a principal target for stabilizing or destabilizing signals that ultimately result in synapse maintenance or elimination.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/05/20 alle ore 14:43:02