| pubmed-article:11438592 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11438592 | lifeskim:mentions | umls-concept:C1622186 | lld:lifeskim |
| pubmed-article:11438592 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:11438592 | lifeskim:mentions | umls-concept:C1306673 | lld:lifeskim |
| pubmed-article:11438592 | lifeskim:mentions | umls-concept:C1326514 | lld:lifeskim |
| pubmed-article:11438592 | lifeskim:mentions | umls-concept:C1704788 | lld:lifeskim |
| pubmed-article:11438592 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:11438592 | pubmed:dateCreated | 2001-7-4 | lld:pubmed |
| pubmed-article:11438592 | pubmed:abstractText | 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 to F-actin depolymerization. The decrease in synapse dependence on F-actin correlates well with the acquisition and retention of presynaptic scaffolding proteins 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. | lld:pubmed |
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| pubmed-article:11438592 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11438592 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:11438592 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11438592 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:11438592 | pubmed:issn | 1529-2401 | lld:pubmed |
| pubmed-article:11438592 | pubmed:author | pubmed-author:BensonD LDL | lld:pubmed |
| pubmed-article:11438592 | pubmed:author | pubmed-author:ZhangWW | lld:pubmed |
| pubmed-article:11438592 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:11438592 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11438592 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11438592 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11438592 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11438592 | pubmed:pagination | 5169-81 | lld:pubmed |
| pubmed-article:11438592 | pubmed:dateRevised | 2011-9-22 | lld:pubmed |
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| pubmed-article:11438592 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11438592 | pubmed:articleTitle | Stages of synapse development defined by dependence on F-actin. | lld:pubmed |
| pubmed-article:11438592 | pubmed:affiliation | Fishberg Research Center for Neurobiology and Program in Cell Adhesion, The Mount Sinai School of Medicine, New York, New York 10029, USA. | lld:pubmed |
| pubmed-article:11438592 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11438592 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11438592 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:11438592 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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