The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Interaction of Junctional Adhesion Molecule with the Tight Junction Components ZO-1, Cingulin, and Occludin
Open accessAbstract
Junctional adhesion molecule (JAM) is an integral membrane protein that has been reported to colocalize with the tight junction molecules occludin, ZO-1, and cingulin. However, evidence for the association of JAM with these molecules is missing. Transfection of Chinese hamster ovary cells with JAM (either alone or in combination with occludin) resulted in enhanced junctional localization of both endogenous ZO-1 and cotransfected occludin. Additionally, JAM was coprecipitated with ZO-1 in the detergent-insoluble fraction of Caco-2 epithelial cells. A putative PDZ-binding motif at the cytoplasmic carboxyl terminus of JAM was required for mediating the interaction of JAM with ZO-1, as assessed by in vitro binding and coprecipitation experiments. JAM was also coprecipitated with cingulin, another cytoplasmic component of tight junctions, and this association required the amino-terminal globular head of cingulin. Taken together, these data indicate that JAM is a component of the multiprotein complex of tight junctions, which may facilitate junction assembly.
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Cites
Occludin: a novel integral membrane protein localizing at tight junctions.
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Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
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Itoh, M., Nagafuchi, A., Moroi, S., & Tsukita, S. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.138.1.181 · Cited by 677
Cited by
Regulation of Tight Junction Permeability by Intestinal Bacteria and Dietary Components1,2
Ulluwishewa, D., Anderson, R. C., McNabb, W. C., Moughan, P. J., Wells, J. M., & Roy, N. C. (2011) · The Journal of Nutrition · doi:10.3945/jn.110.135657 · Cited by 1,177
González-Mariscal, L., Betanzos, A., Nava, P., & Jaramillo, B. E. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(02)00037-8 · Cited by 1,160
Blood-brain barrier tight junction permeability and ischemic stroke
Sandoval, K. E., & Witt, K. A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.005 · Cited by 964
Tight Junctions and Cell Polarity
Shin, K., Fogg, V. C., & Margolis, B. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104219 · Cited by 745
Luissint, A.-C., Artus, C., Glacial, F., Ganeshamoorthy, K., & Couraud, P.-O. (2012) · Fluids and Barriers of the CNS · doi:10.1186/2045-8118-9-23 · Cited by 654
“ZO proteins interact with the C-terminal domain of claudins via their first PDZ domain (PDZ1) [57], to JAMs by the third PDZ domain (PDZ3) [58] and to occludin via their GUK domains [55,56,59].”
Metadata
- Authors
- Bazzoni, G., Martı́nez-Estrada, O. M., Orsenigo, F., Cordenonsi, M., Citi, S., & Dejana, E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 275
- Issue
- 27
- Pages
- 20520-20526
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2042652697
- Cited by
- 480
- References
- 4
- FWCI
- 14.08
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Bazzoni, G., Martı́nez-Estrada, O. M., Orsenigo, F., Cordenonsi, M., Citi, S., & Dejana, E. (2000). Interaction of Junctional Adhesion Molecule with the Tight Junction Components ZO-1, Cingulin, and Occludin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m905251199
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.