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  • Title: Caveolin binds independently to claudin-2 and occludin.
    Author: Itallie CM, Anderson JM.
    Journal: Ann N Y Acad Sci; 2012 Jun; 1257():103-7. PubMed ID: 22671595.
    Abstract:
    Treatment of epithelial and endothelial cells with proinflammatory cytokines can stimulate tight junction protein endocytosis, with associated loss of physiologic barrier function. In some instances, the endocytic scaffolding protein, caveolin-1, has been implicated in the cytokine-dependent retrieval of the tight junction proteins occludin and claudins. How caveolin-1 interacts with these proteins, however, remains undefined. Using co-immunoprecipitation assays, we found that caveolin-1 separately interacts with claudin-2 and occludin, but not with ZO-1, ZO-2, or claudin-4. Further, we found that the interactions of caveolin-1 with claudin-2 and occludin were not disrupted by cholesterol removal, suggesting that they were not dependent on co-localization to cholesterol-rich lipid rafts. Co-immunoprecipitation of caveolin-1 with chimeras between claudin-2 and -4 indicated that the C-terminal cytoplasmic domain of claudin-2 is required for association with caveolin-1; similar analysis showed that the ZO-1 binding region of occludin is not required for its interaction with caveolin-1. The finding that caveolin-1 interacts with claudin-2 and occludin, but not with claudin-4 or ZO-1, suggests a potential mechanism for selective retrieval of tight junction components.
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