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J. Biol. Chem., Vol. 275, Issue 27, 20520-20526, July 7, 2000
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From the 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.
Interaction of Junctional Adhesion Molecule with the Tight
Junction Components ZO-1, Cingulin, and Occludin*
§¶,§
,,
Istituto di Ricerche Farmacologiche Mario
Negri, 20157 Milano, Italy, ** Università di Padova,
Dipartimento di Biologia, 35121 Padova, Italy, and
Università degli Studi
dell'Insubria, Dipartimento di Scienze Cliniche e Biologiche,
Facoltà di Medicina e Chirurgia, 21100 Varese, Italy
*
This work was supported in part by Human Frontiers Science
Program Grant RG 0006/1997-M; EEC Grants BIO4 CT 980337, BMH4 CT 983380, QLGL-CT-1999-01036, and QLK3-CT-1999-00020; Consiglio Nazionale
delle Ricerche Grant 97.01299.PF49, and Associazone Italiana per la
Ricerca sul Cancro.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Recipient of a fellowship from International Centre for Genetic
Engineering and Biotechnology, Trieste, Italy.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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M. Itoh, H. Sasaki, M. Furuse, H. Ozaki, T. Kita, and S. Tsukita Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions J. Cell Biol., August 6, 2001; 154(3): 491 - 498. [Abstract] [Full Text] [PDF]
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 J. M. Anderson Molecular Structure of Tight Junctions and Their Role in Epithelial Transport Physiology, June 1, 2001; 16(3): 126 - 130. [Abstract] [Full Text] [PDF]
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E. S. Wittchen, J. Haskins, and B. R. Stevenson Exogenous Expression of the Amino-terminal Half of the Tight Junction Protein ZO-3 Perturbs Junctional Complex Assembly J. Cell Biol., November 13, 2000; 151(4): 825 - 836. [Abstract] [Full Text] [PDF]
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S. A. Cunningham, M. P. Arrate, J. M. Rodriguez, R. J. Bjercke, P. Vanderslice, A. P. Morris, and T. A. Brock A Novel Protein with Homology to the Junctional Adhesion Molecule. CHARACTERIZATION OF LEUKOCYTE INTERACTIONS J. Biol. Chem., October 27, 2000; 275(44): 34750 - 34756. [Abstract] [Full Text] [PDF]
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M. Aurrand-Lions, L. Duncan, C. Ballestrem, and B. A. Imhof JAM-2, a Novel Immunoglobulin Superfamily Molecule, Expressed by Endothelial and Lymphatic Cells J. Biol. Chem., January 19, 2001; 276(4): 2733 - 2741. [Abstract] [Full Text] [PDF]
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O. M. Martinez-Estrada, A. Villa, F. Breviario, F. Orsenigo, E. Dejana, and G. Bazzoni Association of Junctional Adhesion Molecule with Calcium/calmodulin-dependent Serine Protein Kinase (CASK/LIN-2) in Human Epithelial Caco-2 Cells J. Biol. Chem., March 16, 2001; 276(12): 9291 - 9296. [Abstract] [Full Text] [PDF]
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Y. Hamazaki, M. Itoh, H. Sasaki, M. Furuse, and S. Tsukita Multi-PDZ Domain Protein 1 (MUPP1) Is Concentrated at Tight Junctions through Its Possible Interaction with Claudin-1 and Junctional Adhesion Molecule J. Biol. Chem., January 4, 2002; 277(1): 455 - 461. [Abstract] [Full Text] [PDF]
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