Tight Junction Protein 2 (Zona Occludens 2) Proteins (TJP2)

Human Tight Junction Protein 2 (Zona Occludens 2) (TJP2) interaction partners

1. Results suggested that a reduction in CLDN18-dependent ZO-2 expression enhances MMP2 expression in lung adenocarcinoma cells, resulting in the promotion of the cell migration.

2. Mutations in the genes responsible for PFIC may be involved in both young and adults with cryptogenic cholestasis in a considerable number of cases, including in heterozygous status.

3. Biochemistry and microscopy approaches in T cells confirmed SNX27/ZO-2 PDZ-dependent interaction, and demonstrated its role controlling the dynamic localization of ZO-2 at the IS

4. A likely causal mutation was identified in the majority (61%), spanning many genes including ones that have only rarely been reported to cause cholestatic liver disease, e.g. TJP2 and VIPAS39

5. Patients with a confirmed ABCB11 or tight junction protein 2 gene mutation (n = 7) had a minimally detectable THBA proportion (0.23-2.99% of total BAs). Three patients with an ATP8B1 mutation had an elevated THBA proportion (7.51-37.26%).

6. Studies indicate the modular and supramodular organization of zonula occludens protein 2 (ZO-2) that allows it to interact with a wide variety of molecules, including cell-cell adhesion proteins, cytoskeletal components, and nuclear factors.

7. Data identified two Disease-causing Genes TJP2 and GJB2 in a Chinese Family with Unconditional Autosomal Dominant Nonsyndromic Hereditary Hearing Impairment.

8. TJP2 deficiency may predispose to hepatocellular carcinoma in early childhood

9. Claudin-19, the most abundant claudin in myelin, exhibited no binding to ZO2.

10. JAM-A regulates epithelial permeability via association with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and control contraction of the apical cytoskeleton.

11. Protein-truncating mutations in the tight junction protein 2 gene cause failure of protein localization and disruption of tight-junction structure, leading to severe cholestatic liver disease.

12. demonstrated that ZO-2 inhibition increases invasive and migrative capacities of invasive tumor cells. This was associated with an increase of MT1-MMP

13. the Alu-related transcript of TJP2 gene (TJP2-Alu transcript) was differentially expressed between colorectal tumor and normal tissues; potential diagnostic markers for colorectal cancer.

14. ZO-2 inhibits the Wnt signaling pathway, reduces cell proliferation, and promotes apoptosis; its absence, mutation, or overexpression is present in various human diseases, including deafness and cancer.

15. AmotL1 and ZO-2 are two candidates that could be harnessed to control the oncogenic function of YAP.

16. these findings imply involvement of the ZO-2 tight junction independent signaling complex containing Jak1 and uPAR in VSMC intercellular communications.

17. ZO-2 interacts with YAP2 to form complex; ZO-2 facilitates both nuclear translocation of YAP2 & pro-apoptotic function of YAP2; YAP2/ZO-2 complex appears to be involved in cell detachment

18. The identification of ZASP helps to unfold the complex nuclear molecular arrays that form on ZO-2 scaffolds.

19. the first PDZ domain of zona occludens-1 (ZO-1) and 2 (ZO-2) interacts with the carboxy-terminal PDZ binding motif of TAZ

20. TJP2- and GSK-3beta-mediated increased susceptibility to apoptosis of cells of the inner ear is the mechanism for adult-onset hearing loss in this kindred and may serve as one model for age-related hearing loss in the general population.

Mouse (Murine) Tight Junction Protein 2 (Zona Occludens 2) (TJP2) interaction partners

1. Based on results obtained in cultured epithelial cells transfected with ZO-2 mutated at a MET target lysine residue.

2. Podocyte-specific deletion of the ZO-2 gene did not cause overt defects; however, double knockout of ZO-1 and ZO-2 genes accelerated the defects observed in ZO-1 knockout mice. These results suggest that ZO-2 plays supportive roles in the ZO-1-dependent regulation of podocyte filtration barrier.

3. In the present study, we found that the protein level of ZO-2, a scaffolding tight junction protein, decreased in the bladder of OVX mice indicating a possible role in overactive bladder.

4. Expression of Podocalyxin, which positively regulates the formation of microvilli and the apical membrane, is repressed in embryoid bodies lacking both ZO-1 and ZO-2 and this correlates with an aberrant submembranous localization of Ezrin.

5. SNX27 associates with ZO-2 and modulates the epithelial tight junction.

6. ZO-2 protects against podocyte dysfunction induced by adreiamycin. This action is regulated by ZO-2-mediated inhibition of the Wnt/beta-catenin signaling pathway

7. the first PDZ domain of ZO-2 interacts with YAP2 to form complex; ZO-2 facilitates both nuclear translocation of YAP2 & pro-apoptotic function of YAP2; these activities of ZO-2 are PDZ-domain-dependent

8. Male ZO-2 chimeras show reduced fertility and pathological changes in the testis. Lanthanum tracer experiments show a compromised blood-testis barrier.

9. nuclear ZO-2 is present in epithelial and endothelial cells, particularly in response to environmental stress conditions

10. ZO-1 and ZO-2 function redundantly to some extent in junction formation/epithelial polarization but they are not functionally identical

11. These findings indicate that ZO-1 and ZO-2 can independently determine whether and where claudins are polymerized.

12. These results suggest novel roles for ZO proteins as Src/Csk scaffolds potentially involved in the regulation of Src transformation.

13. Early embryonic lethality of mice lacking Tjp2, but not Tjp3, reveal critical and nonredundant roles for individual zonula occludens proteins in mammalian development.

14. analysis of ZO-1- and ZO-2-dependent integration of myosin-2 to epithelial zonula

15. Quantitative analysis of trophectoderm tight junctions in ZO-2-deficient embryos revealed increased assembly of ZO-1 but not occludin, indicating ZO protein redundancy as a compensatory mechanism contributing to the mild phenotype observed.

16. ZO-2 play pivotal roles in the final establishment of the belt-like adherens junctions (zonula adherens), followed by the formation of the belt-like TJs (zonula occludens) with paracellular barrier function

Zebrafish Tight Junction Protein 2 (Zona Occludens 2) (TJP2) interaction partners

1. analysis of tissue distribution and developmental expression of tjp1/zo-1, tjp2/zo-2 and tjp3/zo-3 in the zebrafish, Danio rerio