The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
Junctional adhesion molecules (JAMs): more molecules with dual functions?
Abstract
Junctional adhesion molecules (JAMs) are members of an immunoglobulin subfamily expressed by leukocytes and platelets as well as by epithelial and endothelial cells, in which they localize to cell-cell contacts and are specifically enriched at tight junctions. The recent identification of extracellular ligands and intracellular binding proteins for JAMs suggests two functions for JAMs. JAMs associate through their extracellular domains with the leukocyte β2 integrins LFA-1 and Mac-1 as well as with the β1 integrin α4β1. All three integrins are involved in the regulation of leukocyte-endothelial cell interactions. Through their cytoplasmic domains, JAMs directly associate with various tight junction-associated proteins including ZO-1, AF-6, MUPP1 and the cell polarity protein PAR-3. PAR-3 is part of a ternary protein complex that contains PAR-3, atypical protein kinase C and PAR-6. This complex is highly conserved through evolution and is involved in the regulation of cell polarity in organisms from Caenorhabditis elegans and Drosophila to vertebrates. These findings point to dual functions for JAMs: they appear to regulate both leukocyte/platelet/endothelial cell interactions in the immune system and tight junction formation in epithelial and endothelial cells during the acquisition of cell polarity.
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Cites
Lymphocyte Homing and Homeostasis
Butcher, E. C., & Picker, L. J. (1996) · Science · doi:10.1126/science.272.5258.60 · Cited by 2,846
Comparative Genomics of the Eukaryotes
Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M., & Cantley, L. C. (1997) · Science · doi:10.1126/science.275.5296.73 · Cited by 1,385
The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
Joberty, G., Petersen, C., Gao, L., & Macara, I. G. (2000) · Nature Cell Biology · doi:10.1038/35019573 · Cited by 928 · cited 1×
“Vertebrate PAR-3 (also known as ASIP) (Izumi et al., 1998) localizes to the TJs of epithelial cells and forms a complex with atypical protein kinase C (aPKC) and PAR-6 (Joberty et al., 2000; Johansson et al., 2000; Lin et al., 2000; Qiu et al., 2000; Suzuki et al., 2001) (Fig.”
BackgroundA mammalian PAR-3–PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
Lin, D., Edwards, A. S., Fawcett, J. P., Mbamalu, G., Scott, J. D., & Pawson, T. (2000) · Nature Cell Biology · doi:10.1038/35019582 · Cited by 743
Integrated activity of PDZ protein complexes regulates epithelial polarity
Bilder, D., Schober, M., & Perrimon, N. (2003) · Nature Cell Biology · doi:10.1038/ncb897 · Cited by 435
Yamanaka, T., Horikoshi, Y., Suzuki, A., Sugiyama, Y., Kitamura, K., Maniwa, R., Nagai, Y., Yamashita, A., Hirose, T., Ishikawa, H., et al. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00453.x · Cited by 306
Self-citationSuzuki, A., Ishiyama, C., Hashiba, K., Shimizu, M., Ebnet, K., & Ohno, S. (2002) · Journal of Cell Science · doi:10.1242/jcs.00032 · Cited by 251
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Intestinal barrier function: molecular regulation and disease pathogenesis
Groschwitz, K. R., & Hogan, S. P. (2009) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2009.05.038 · Cited by 1,775
Inflammatory cells during wound repair: the good, the bad and the ugly
Martin, P., & Leibovich, S. J. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.09.002 · Cited by 1,340
Tight junctions/adherens junctions: basic structure and function
Niessen, C. M. (2007) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700865 · Cited by 756
Klaassen, I., Van Noorden, C. J. F., & Schlingemann, R. O. (2013) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2013.02.001 · Cited by 722
Martini, E., Krug, S. M., Siegmund, B., Neurath, M. F., & Becker, C. (2017) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2017.03.007 · Cited by 668
Metadata
- Authors
- Ebnet, K., Suzuki, A., Ohno, S., & Vestweber, D.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2004-01-01
- Volume
- 117
- Issue
- 1
- Pages
- 19-29
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2157055702
- Cited by
- 501
- References
- 8
- FWCI
- 12.79
- Type
- journal article
- Language
- en
- Open access
- closed
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