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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2005-8-15
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pubmed:abstractText |
N-cadherin is an adhesion receptor that participates in both interaction between immature pre- and postsynaptic neurons and in the stabilization and function of matured neuron-neuron synapses. To better understand how the N-cadherin complex contributes to synapse formation, we examined its distribution and composition during synapse formation in the chick ciliary neurons. It was found that at early phases of synaptogenesis, N-cadherin is distributed in small clusters on the cell surface and primarily associates with p120-catenin and beta-catenin. In contrast, as synaptic contacts matured, larger N-cadherin clusters were found localized adjacent to the active zone and associated with PS1 and gamma-catenin, while p120- and beta-catenin were dispersed among other cell regions, including axons. As it is known that PS1 binds gamma-catenin and that uncoupled p120-catenin can alter the cytoskeleton via its effect on Rho GTPases, these changes in the molecular composition of the N-cadherin complex (represented by the uncoupling of p120-catenin and association with PS1) may correspond to distinct functional states of the complex involved in synaptic maturation.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadherins,
http://linkedlifedata.com/resource/pubmed/chemical/Catenins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Desmoplakins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Presenilin-1,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/delta catenin,
http://linkedlifedata.com/resource/pubmed/chemical/gamma Catenin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1044-7431
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
30
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
118-30
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:16046145-Animals,
pubmed-meshheading:16046145-CHO Cells,
pubmed-meshheading:16046145-Cadherins,
pubmed-meshheading:16046145-Catenins,
pubmed-meshheading:16046145-Cell Adhesion Molecules,
pubmed-meshheading:16046145-Cell Differentiation,
pubmed-meshheading:16046145-Chick Embryo,
pubmed-meshheading:16046145-Chickens,
pubmed-meshheading:16046145-Cricetinae,
pubmed-meshheading:16046145-Cytoskeletal Proteins,
pubmed-meshheading:16046145-Desmoplakins,
pubmed-meshheading:16046145-Green Fluorescent Proteins,
pubmed-meshheading:16046145-Membrane Proteins,
pubmed-meshheading:16046145-Microscopy, Immunoelectron,
pubmed-meshheading:16046145-Neurons,
pubmed-meshheading:16046145-Phosphoproteins,
pubmed-meshheading:16046145-Presenilin-1,
pubmed-meshheading:16046145-Synapses,
pubmed-meshheading:16046145-Trans-Activators,
pubmed-meshheading:16046145-Transfection,
pubmed-meshheading:16046145-beta Catenin,
pubmed-meshheading:16046145-gamma Catenin
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pubmed:year |
2005
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pubmed:articleTitle |
Assembly of the N-cadherin complex during synapse formation involves uncoupling of p120-catenin and association with presenilin 1.
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pubmed:affiliation |
Department of Physiology and Neurobiology, The University of Connecticut, 3107 Horsebarn Hill Road, Storrs, CT 06269, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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