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Guanylyl Cyclase C Receptor: Regulation of Catalytic Activity by ATP

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Bioscience Reports

Abstract

Guanylyl cyclase C (GCC), a member of the family of membrane bound guanylyl cyclases is the receptor for the heat-stable enterotoxin (ST) peptides and the guanylin family of endogenous peptides. GCC is activated upon ligand binding to increase intracellular cGMP levels, which in turn activates other downstream signalling events in the cell. GCC is also activated in vitro by nonionic detergents. We have used the T84 cell line as a model system to investigate the regulation of GCC activity by ATP. Ligand-stimulated GCC activity is potentiated in the presence of ATP, whereas detergent-stimulated activity is inhibited. The potentiation of GCC activity by ATP is dependent on the presence of Mg2+ ions, and is probably brought about by a direct binding of Mg-ATP to GCC. The protein kinase-like domain of GCC, which has earlier been shown to play a critical role in the regulation of GCC activity, may be a possible site for the binding of Mg-ATP to GCC.

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Authors and Affiliations

  1. Department of Molecular Reproduction, Development and Genetics, Indian Institute of Science, Bangalore, 560 012, India

    Rashna Bhandari & Sandhya S. Visweswariah

  2. Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India

    K. Suguna

Authors
  1. Rashna Bhandari
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  2. K. Suguna
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  3. Sandhya S. Visweswariah
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Bhandari, R., Suguna, K. & Visweswariah, S.S. Guanylyl Cyclase C Receptor: Regulation of Catalytic Activity by ATP. Biosci Rep 19, 179–188 (1999). https://doi.org/10.1023/A:1020273619211

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