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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator
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Protein phosphatase 2C dephosphorylates and inactivates cystic fibrosis transmembrane conductance regulator

机译：蛋白磷酸酶2C使磷酸化并使囊性纤维化跨膜电导调节剂失活

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摘要

cAMP-dependent phosphorylation activates the cystic fibrosis transmembrane conductance regulator (CFTR) in epithelia. However, the protein phosphatase (PP) that dephosphorylates and inactivates CFTR in airway and intestinal epithelia, two major sites of disease, is not certain. We found that in airway and colonic epithelia, neither okadaic acid nor FK506 prevented inactivation of CFTR when cAMP was removed. These results suggested that a phosphatase distinct from PP1, PP2A, and PP2B was responsible. Because PP2C is insensitive to these inhibitors, we tested the hypoth- esis that it regulates CFTR. We found that PP2C is expressed in airway and T84 intestinal epithelia.
机译：cAMP依赖性磷酸化激活上皮细胞的囊性纤维化跨膜电导调节剂（CFTR）。然而，尚不清楚使疾病的两个主要部位气道和肠上皮中的CFTR脱磷酸并使CFTR失活的蛋白磷酸酶（PP）。我们发现，在气道和结肠上皮中，冈田酸和FK506都不能在移除cAMP时阻止CFTR失活。这些结果表明，不同于PP1，PP2A和PP2B的磷酸酶起作用。因为PP2C对这些抑制剂不敏感，所以我们检验了它调节CFTR的假设。我们发现PP2C在气道和T84肠上皮细胞中表达。

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