Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-8-7
pubmed:abstractText
At tight junctions (TJs), claudins with four transmembrane domains are incorporated into TJ strands. Junctional adhesion molecule (JAM), which belongs to the immunoglobulin superfamily, is also localized at TJs, but it remains unclear how JAM is integrated into TJs. Immunoreplica electron microscopy revealed that JAM showed an intimate spatial relationship with TJ strands in epithelial cells. In L fibroblasts expressing exogenous JAM, JAM was concentrated at cell-cell adhesion sites, where there were no strand-like structures, but rather characteristic membrane domains free of intramembranous particles were detected. These domains were specifically labeled with anti-JAM polyclonal antibody, suggesting that JAM forms planar aggregates through their lateral self-association. Immunofluorescence microscopy and in vitro binding assays revealed that ZO-1 directly binds to the COOH termini of claudins and JAM at its PDZ1 and PDZ3 domains, respectively. Furthermore, another PDZ-containing polarity-related protein, PAR-3, was directly bound to the COOH terminus of JAM, but not to that of claudins. These findings led to a molecular architectural model for TJs: small aggregates of JAM are tethered to claudin-based strands through ZO-1, and these JAM aggregates recruit PAR-3 to TJs. We also discuss the importance of this model from the perspective of the general molecular mechanisms behind the recruitment of PAR proteins to plasma membranes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10395639, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10508648, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10601346, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10698320, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10779521, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10830161, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10852816, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10873802, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10877843, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10913139, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10934474, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-10934475, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-11257119, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-11283726, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-2014265, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-3345562, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-3528172, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-4611943, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-7485497, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8132716, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8276896, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8395056, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8408213, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8486731, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8586656, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-8791533, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-9531559, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-9647647, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-9660867, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-9763423, http://linkedlifedata.com/resource/pubmed/commentcorrection/11489913-9786950
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9525
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-7
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11489913-Animals, pubmed-meshheading:11489913-Cell Adhesion, pubmed-meshheading:11489913-Cell Adhesion Molecules, pubmed-meshheading:11489913-Cell Polarity, pubmed-meshheading:11489913-Cells, Cultured, pubmed-meshheading:11489913-Epithelial Cells, pubmed-meshheading:11489913-Fibroblasts, pubmed-meshheading:11489913-Freeze Fracturing, pubmed-meshheading:11489913-Membrane Proteins, pubmed-meshheading:11489913-Mice, pubmed-meshheading:11489913-Mutagenesis, pubmed-meshheading:11489913-Phosphoproteins, pubmed-meshheading:11489913-Protein Binding, pubmed-meshheading:11489913-Protein Structure, Tertiary, pubmed-meshheading:11489913-Receptors, Thrombin, pubmed-meshheading:11489913-Signal Transduction, pubmed-meshheading:11489913-Tight Junctions, pubmed-meshheading:11489913-Transfection
pubmed:year
2001
pubmed:articleTitle
Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions.
pubmed:affiliation
1Department of Cell Biology, Faculty of Medicine, Kyoto University, Kyoto 606-8501, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't