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Predicate | Object |
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rdf:type | |
pubmed:issue |
4
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pubmed:dateCreated |
1998-10-14
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pubmed:abstractText |
Neurexins are neuronal cell-surface proteins with up to thousands of isoforms. These isoforms are generated by alternative splicing of transcripts from six promoters in three genes. The structure of neurexins resembles cell-surface receptors with a modular architecture suggestive of a sequential assembly during evolution. Neurexins probably perform multiple functions in the brain. They participate in intercellular junctions in which beta-neurexins tightly bind to a second class of neuronal cell-surface receptors called neuroligins. Intracellularly, the neurexin/neuroligin junction is bound by CASK on the neurexin side and PSD95 on the neuroligin side. CASK and PSD95 are homologous membrane-associated guanylate kinases that bind to the neurexin/neuroligin junction via PDZ domains, creating an asymmetric junction (neurexin/neuroligin) with similar intracellular binding partners. In addition to a function as cell-adhesion molecules, neurexins may also serve as a signalling receptor, because a class of ligands for alpha-neurexins called neurexophilins is similar to peptide hormones. Finally, at least one neurexin isoform, neurexin Ialpha, represents a high-affinity receptor for alpha-latrotoxin, which is a potent excitatory neurotoxin. Thus, neurexins constitute a large family of neuronal receptors that may be involved in multiple interactive functions between neurons.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/neurexin II,
http://linkedlifedata.com/resource/pubmed/chemical/neurexin IIIalpha,
http://linkedlifedata.com/resource/pubmed/chemical/neurexophilin
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0022-3042
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
71
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1339-47
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9751164-Amino Acid Sequence,
pubmed-meshheading:9751164-Animals,
pubmed-meshheading:9751164-Glycoproteins,
pubmed-meshheading:9751164-Humans,
pubmed-meshheading:9751164-Molecular Sequence Data,
pubmed-meshheading:9751164-Nerve Tissue Proteins,
pubmed-meshheading:9751164-Neuropeptides,
pubmed-meshheading:9751164-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
The making of neurexins.
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pubmed:affiliation |
Department of Molecular Genetics and Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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