Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-10-13
pubmed:databankReference
pubmed:abstractText
We identify a complex of three proteins in brain that has the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion. The three proteins are: (1) CASK, a protein related to MAGUKs (membrane-associated guanylate kinases); (2) Mint1, a putative vesicular trafficking protein; and (3) Veli1, -2, and -3, vertebrate homologs of C. elegans LIN-7. CASK, Mint1, and Velis form a tight, salt-resistant complex that can be readily isolated. CASK, Mint1, and Velis contain PDZ domains in addition to other modules. However, no PDZ domains are involved in complex formation, leaving them free to recruit cell adhesion molecules, receptors, and channels to the complex. We propose that the tripartite complex acts as a nucleation site for the assembly of proteins involved in synaptic vesicle exocytosis and synaptic junctions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/APBA1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing, http://linkedlifedata.com/resource/pubmed/chemical/Apba1 protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Apba1 protein, rat, http://linkedlifedata.com/resource/pubmed/chemical/CASK kinases, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent..., http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DLG2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanylate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Helminth Proteins, http://linkedlifedata.com/resource/pubmed/chemical/LIN-7 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Nucleoside-Phosphate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Synaptophysin, http://linkedlifedata.com/resource/pubmed/chemical/Synaptotagmins, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/neurexin Ibeta, http://linkedlifedata.com/resource/pubmed/chemical/neurexophilin
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
94
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
773-82
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:9753324-Adaptor Proteins, Signal Transducing, pubmed-meshheading:9753324-Animals, pubmed-meshheading:9753324-Brain Chemistry, pubmed-meshheading:9753324-Caenorhabditis elegans, pubmed-meshheading:9753324-Caenorhabditis elegans Proteins, pubmed-meshheading:9753324-Calcium-Binding Proteins, pubmed-meshheading:9753324-Calcium-Calmodulin-Dependent Protein Kinases, pubmed-meshheading:9753324-Carrier Proteins, pubmed-meshheading:9753324-Cell Adhesion, pubmed-meshheading:9753324-Cell Membrane, pubmed-meshheading:9753324-Cloning, Molecular, pubmed-meshheading:9753324-Exocytosis, pubmed-meshheading:9753324-Glycoproteins, pubmed-meshheading:9753324-Guanylate Kinase, pubmed-meshheading:9753324-Helminth Proteins, pubmed-meshheading:9753324-Humans, pubmed-meshheading:9753324-Membrane Glycoproteins, pubmed-meshheading:9753324-Membrane Proteins, pubmed-meshheading:9753324-Mice, pubmed-meshheading:9753324-Molecular Sequence Data, pubmed-meshheading:9753324-Nerve Tissue Proteins, pubmed-meshheading:9753324-Neurons, pubmed-meshheading:9753324-Neuropeptides, pubmed-meshheading:9753324-Nucleoside-Phosphate Kinase, pubmed-meshheading:9753324-Protein Binding, pubmed-meshheading:9753324-Rats, pubmed-meshheading:9753324-Sequence Homology, Amino Acid, pubmed-meshheading:9753324-Synaptic Vesicles, pubmed-meshheading:9753324-Synaptophysin, pubmed-meshheading:9753324-Synaptotagmins, pubmed-meshheading:9753324-Tumor Suppressor Proteins, pubmed-meshheading:9753324-Vesicular Transport Proteins
pubmed:year
1998
pubmed:articleTitle
A tripartite protein complex with the potential to couple synaptic vesicle exocytosis to cell adhesion in brain.
pubmed:affiliation
Center for Basic Neuroscience, Department of Molecular Genetics, Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center at Dallas, 75235, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't