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Atrial natriuretic factor-receptor guanylate cyclase signal transduction mechanism

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Abstract

Atrial natriuretic factor (ANF) receptor guanylate cyclase (ANF-RGC), like the other members of the membrane guanylate cyclase family, is a single transmembrane-spanning protein. The transmembrane domain separates the protein into two regions, extracellular and intracellular. The extracellular region contains the ANF-binding domain and the intracellular region the catalytic domain located at the C-terminus of the protein. Preceding the catalytic domain, the intracellular region is comprised of the following functional domains: juxtaposed 40 amino acids to the transmembrane domain is the ATP-regulated module (ARM) domain [also termed the kinase homology domain (KHD)], and the putative dimerization domain. The ANF-RGC signaling is initiated by hormone, ANF, binding to its extracellular binding site. The binding signal is transduced through the transmembrane domain to the intracellular portion where ATP binding to the ARM domain partially activates the cyclase and prepares it for subsequent steps involving phosphorylation and attaining the fully activated state. This chapter reviews the signaling modules of ANF-RGC.

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Acknowledgments

This research was supported by NIH award LH 084584. I wish to express my sincere gratefulness to Dr. Rameshwar K. Sharma, Distinguished Professor, Salus University, for introducing me to the membrane guanylate cyclase transduction research, for years of guidance, support, and collaboration.

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  1. The Unit of Regulatory and Molecular Biology, Research Divisions of Biochemistry and Molecular Biology, Salus University, Elkins Park, PA, 19027, USA

    Teresa Duda

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  1. Teresa Duda
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Correspondence to Teresa Duda.

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Duda, T. Atrial natriuretic factor-receptor guanylate cyclase signal transduction mechanism. Mol Cell Biochem 334, 37–51 (2010). https://doi.org/10.1007/s11010-009-0335-7

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  • DOI: https://doi.org/10.1007/s11010-009-0335-7

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