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TJP2  -  tight junction protein 2

Homo sapiens

Synonyms: C9DUPq21.11, DFNA51, DUP9q21.11, PFIC4, Tight junction protein 2, ...
 
 
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Disease relevance of TJP2

 

High impact information on TJP2

  • Inheritance seems to be oligogenic, with genotype at BAAT modifying penetrance in individuals homozygous with respect to the mutation in TJP2 [3].
  • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins [4].
  • ZO-1, ZO-2, and ZO-3, which contain three PDZ domains (PDZ1 to -3), are concentrated at tight junctions (TJs) in epithelial cells [4].
  • A polyclonal antiserum was raised against a unique region of ZO-2 and found to exclusively label the cytoplasmic surfaces of tight junctions in MDCK plasma membrane preparations, indicating that ZO-2 is a tight junction-associated protein [5].
  • The deduced amino acid sequence revealed that canine ZO-2 contains a region that is very similar to sequences in human and mouse ZO-1 [5].
 

Biological context of TJP2

 

Anatomical context of TJP2

 

Associations of TJP2 with chemical compounds

  • Between the first and second PDZ domains, ZO-2 displays a basic region (pI = 10.27) containing 22% arginine residues [16].
  • Coincidently, ZO-1 and another tight junction protein, ZO-2, become transiently phosphorylated on tyrosine residues, as determined by anti-phosphotyrosine immunoblotting [17].
  • These changes reversed after ATP repletion, and the movement of insoluble occludin, ZO-1, and ZO-2 back into the soluble pool was again via a genistein-sensitive mechanism [18].
 

Physical interactions of TJP2

 

Other interactions of TJP2

 

Analytical, diagnostic and therapeutic context of TJP2

  • Sequence analysis of multiple ZO-2 cDNAs reveals a 36-amino acid domain in this C-terminal region present in only some of the cDNAs [16].
  • Immunofluorescence microscopy and immunoblot analysis showed that activated PMN adhesion to resting monolayers or PMN migration across interleukin-1-treated monolayers does not result in widespread proteolytic loss of TJ proteins (ZO-1, ZO-2, and occludin) from endothelial borders [24].
  • Semi-quantitative RT-PCR analysis of human ZO-2 revealed a striking difference in the expression of various regions of the ZO-2 transcript in normal and neoplastic cells and the presence of an abnormality at the 5'-end of mRNA [12].
  • Furthermore, immunoprecipitation experiments revealed that the second PDZ domain of ZO-2 was directly associated with N-ZO-1 [14].
  • Our results from two-hybrid assays and in vivo co-immunoprecipitation studies provide evidence to suggest that ZO-2 associates with the C-terminal portion of SAF-B via its PDZ-1 domain [13].

References

  1. Organization and expression of the human zo-2 gene (tjp-2) in normal and neoplastic tissues. Chlenski, A., Ketels, K.V., Korovaitseva, G.I., Talamonti, M.S., Oyasu, R., Scarpelli, D.G. Biochim. Biophys. Acta (2000) [Pubmed]
  2. Altered expression of ZO-1 and ZO-2 in sertoli cells and loss of blood-testis barrier integrity in testicular carcinoma in situ. Fink, C., Weigel, R., Hembes, T., Lauke-Wettwer, H., Kliesch, S., Bergmann, M., Brehm, R.H. Neoplasia (2006) [Pubmed]
  3. Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Carlton, V.E., Harris, B.Z., Puffenberger, E.G., Batta, A.K., Knisely, A.S., Robinson, D.L., Strauss, K.A., Shneider, B.L., Lim, W.A., Salen, G., Morton, D.H., Bull, L.N. Nat. Genet. (2003) [Pubmed]
  4. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. Itoh, M., Furuse, M., Morita, K., Kubota, K., Saitou, M., Tsukita, S. J. Cell Biol. (1999) [Pubmed]
  5. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. Jesaitis, L.A., Goodenough, D.A. J. Cell Biol. (1994) [Pubmed]
  6. Developmental regulation of claudin localization by fetal alveolar epithelial cells. Daugherty, B.L., Mateescu, M., Patel, A.S., Wade, K., Kimura, S., Gonzales, L.W., Guttentag, S., Ballard, P.L., Koval, M. Am. J. Physiol. Lung Cell Mol. Physiol. (2004) [Pubmed]
  7. In vitro protein complex formation with cytoskeleton-anchoring domain of occludin identified by limited proteolysis. Peng, B.H., Lee, J.C., Campbell, G.A. J. Biol. Chem. (2003) [Pubmed]
  8. Nuclear localization of the tight junction protein ZO-2 in epithelial cells. Islas, S., Vega, J., Ponce, L., González-Mariscal, L. Exp. Cell Res. (2002) [Pubmed]
  9. Protein-binding domains of the tight junction protein, ZO-2, are highly conserved between avian and mammalian species. Collins, J.R., Rizzolo, L.J. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
  10. The Friedreich ataxia critical region spans a 150-kb interval on chromosome 9q13. Montermini, L., Rodius, F., Pianese, L., Moltò, M.D., Cossée, M., Campuzano, V., Cavalcanti, F., Monticelli, A., Palau, F., Gyapay, G. Am. J. Hum. Genet. (1995) [Pubmed]
  11. Interferon-beta counteracts inflammatory mediator-induced effects on brain endothelial cell tight junction molecules-implications for multiple sclerosis. Kuruganti, P.A., Hinojoza, J.R., Eaton, M.J., Ehmann, U.K., Sobel, R.A. J. Neuropathol. Exp. Neurol. (2002) [Pubmed]
  12. Tight junction protein ZO-2 is differentially expressed in normal pancreatic ducts compared to human pancreatic adenocarcinoma. Chlenski, A., Ketels, K.V., Tsao, M.S., Talamonti, M.S., Anderson, M.R., Oyasu, R., Scarpelli, D.G. Int. J. Cancer (1999) [Pubmed]
  13. The tight junction protein ZO-2 localizes to the nucleus and interacts with the heterogeneous nuclear ribonucleoprotein scaffold attachment factor-B. Traweger, A., Fuchs, R., Krizbai, I.A., Weiger, T.M., Bauer, H.C., Bauer, H. J. Biol. Chem. (2003) [Pubmed]
  14. Characterization of ZO-2 as a MAGUK family member associated with tight as well as adherens junctions with a binding affinity to occludin and alpha catenin. Itoh, M., Morita, K., Tsukita, S. J. Biol. Chem. (1999) [Pubmed]
  15. Regulation of cellular and molecular trafficking across human brain endothelial cells by Th1- and Th2-polarized lymphocytes. Biernacki, K., Prat, A., Blain, M., Antel, J.P. J. Neuropathol. Exp. Neurol. (2004) [Pubmed]
  16. The tight junction protein ZO-2 contains three PDZ (PSD-95/Discs-Large/ZO-1) domains and an alternatively spliced region. Beatch, M., Jesaitis, L.A., Gallin, W.J., Goodenough, D.A., Stevenson, B.R. J. Biol. Chem. (1996) [Pubmed]
  17. Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-1 in A431 cells. Van Itallie, C.M., Balda, M.S., Anderson, J.M. J. Cell. Sci. (1995) [Pubmed]
  18. Role of tyrosine phosphorylation in the reassembly of occludin and other tight junction proteins. Tsukamoto, T., Nigam, S.K. Am. J. Physiol. (1999) [Pubmed]
  19. Association of ARVCF with zonula occludens (ZO)-1 and ZO-2: binding to PDZ-domain proteins and cell-cell adhesion regulate plasma membrane and nuclear localization of ARVCF. Kausalya, P.J., Phua, D.C., Hunziker, W. Mol. Biol. Cell (2004) [Pubmed]
  20. Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. Wittchen, E.S., Haskins, J., Stevenson, B.R. J. Biol. Chem. (1999) [Pubmed]
  21. Characterization of the interaction between protein 4.1R and ZO-2. A possible link between the tight junction and the actin cytoskeleton. Mattagajasingh, S.N., Huang, S.C., Hartenstein, J.S., Benz, E.J. J. Biol. Chem. (2000) [Pubmed]
  22. Roles of ZO-1, occludin, and actin in oxidant-induced barrier disruption. Musch, M.W., Walsh-Reitz, M.M., Chang, E.B. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  23. Molecular structure and assembly of the tight junction. Denker, B.M., Nigam, S.K. Am. J. Physiol. (1998) [Pubmed]
  24. Analysis of tight junctions during neutrophil transendothelial migration. Burns, A.R., Bowden, R.A., MacDonell, S.D., Walker, D.C., Odebunmi, T.O., Donnachie, E.M., Simon, S.I., Entman, M.L., Smith, C.W. J. Cell. Sci. (2000) [Pubmed]
 
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