Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin

Peng, Bi Hung; White, Mark A.; Campbell, Gerald A.; Robert, Jebamony J; Lee, J Ching; Sutton, R. Bryan

doi:10.1107/s1744309105007475

Cited by 2 publications

(3 citation statements)

References 16 publications

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“…Likewise, MUPP1 interacts with claudin1 via its 10th PDZ domain, which is highly similar to the 8th PDZ domain of PATJ ( Figure 3B) (70). Interestingly, the C-terminal PDZ-binding motif of claudin1 can also bind to the 1st PDZ domain of ZO3 and conversely, the GUK domain of ZO3 (like that of ZO1 and 2) can bind to the C-terminal fragment (consisting of 150 amino acids) of occludin (71,72). In addition, the targeting of PATJ to tight junctions is abolished when the 6th PDZ domain binding to ZO3 is deleted, which suggests that ZO3 plays an important role in the targeting of PATJ to tight junctions.…”

Section: 2partners Of Patjmentioning

confidence: 89%

Crumbs proteins in epithelial morphogenesis

et al. 2009

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Cell polarity is an essential feature of most eukaryotic cells, especially epithelial cells in multicellular animals. Polarity protein complexes that regulate epithelial organization have been identified. In this review, it is proposed to describe how the Crumbs complex acts in the process of cell polarity and epithelial organization. During the last decade, several partners of Crumbs, an apical transmembrane protein, have been identified and their direct or indirect associations with the cytoplasmic domain of Crumbs have been dissected. In addition, mutants of several of the genes encoding proteins belonging to the Crumbs network have been obtained in animals ranging from flies to mouse, which have led to a better understanding of their functions in vivo. These functions include polarity axis formation, stabilization of epithelial apico-lateral junctions, photoreceptor organization and ciliogenesis. Since human CRUMBS1 mutations are associated with retina degeneration, it has become essential to define Crumbs network and to understand exactly how this network acts in polarized cells, with a view to developing suitable therapeutic approaches for treating this severe degenerative disease.

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Section: 2partners Of Patjmentioning

confidence: 89%

Crumbs proteins in epithelial morphogenesis

et al. 2009

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“…25 Occludin was previously found to interact with ZOs. 41,42,50 In addition, overexpression of occludin in various cultured cells dramatically increases transepithelial electrical resistance 43,44 and cell adhesiveness. 45 These studies indicate that occludin expressed at TJs may increase cell-cell adhesion.…”

Section: Discussionmentioning

confidence: 99%

“…7E). Occludin is well expressed in kidney CD, 24 interacts with ZOs 41,42 and may increase cell adhesiveness. [43][44][45][46] We noticed a remarkable correlation between ZO-3 and occludin expression in proliferating mCCD cl1 cells.…”

Section: Decreased Cell Adhesion By Zo-3 Silencing Relies On a Multifmentioning

confidence: 99%

Different effects of ZO-1, ZO-2 and ZO-3 silencing on kidney collecting duct principal cell proliferation and adhesion

Qiao¹,

Roth²,

Féraille³

et al. 2014

Cell Cycle

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Coordinated cell proliferation and ability to form intercellular seals are essential features of epithelial tissue function. Tight junctions (TJs) classically act as paracellular diffusion barriers. More recently, their role in regulating epithelial cell proliferation in conjunction with scaffolding zonula occludens (ZO) proteins has come to light. The kidney collecting duct (CD) is a model of tight epithelium that displays intense proliferation during embryogenesis followed by very low cell turnover in the adult kidney. Here, we examined the influence of each ZO protein (ZO-1, -2 and -3) on CD cell proliferation. We show that all 3 ZO proteins are strongly expressed in native CD and are present at both intercellular junctions and nuclei of cultured CD principal cells (mCCDcl1). Suppression of either ZO-1 or ZO-2 resulted in increased G0/G1 retention in mCCDcl1 cells. ZO-2 suppression decreased cyclin D1 abundance while ZO-1 suppression was accompanied by increased nuclear p21 localization, the depletion of which restored cell cycle progression. Contrary to ZO-1 and ZO-2, ZO-3 expression at intercellular junctions dramatically increased with cell density and relied on the presence of ZO-1. ZO-3 depletion did not affect cell cycle progression but increased cell detachment. This latter event partly relied on increased nuclear cyclin D1 abundance and was associated with altered β1-integrin subcellular distribution and decreased occludin expression at intercellular junctions. These data reveal diverging, but interconnected, roles for each ZO protein in mCCDcl1 proliferation. While ZO-1 and ZO-2 participate in cell cycle progression, ZO-3 is an important component of cell adhesion.

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Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin

Cited by 2 publications

References 16 publications

Crumbs proteins in epithelial morphogenesis

Crumbs proteins in epithelial morphogenesis

Different effects of ZO-1, ZO-2 and ZO-3 silencing on kidney collecting duct principal cell proliferation and adhesion

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