ArticleBiochemistry2011
Allosteric modification, the primary ATP activation mechanism of atrial natriuretic factor receptor guanylate cyclase.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- The discovery of hidden guanylate cyclases (GCs) in theComputational and structural biotechnology journal · 2023Article
- Multilimbed membrane guanylate cyclase signaling system, evolutionary ladder.Frontiers in molecular neuroscience · 2022Review
- Targeting Receptor Kinases in Colorectal Cancer.Cancers · 2019Review
- The pseudokinase domains of guanylyl cyclase-A and -B allosterically increase the affinity of their catalytic domains for substrate.Science signaling · 2019Article
- CaFrontiers in molecular neuroscience · 2018Article
- The Kinome of Pacific Oyster Crassostrea gigas, Its Expression during Development and in Response to Environmental Factors.PloS one · 2016Article
- Integrative Signaling Networks of Membrane Guanylate Cyclases: Biochemistry and Physiology.Frontiers in molecular neuroscience · 2016Review
- Structures of soluble guanylate cyclase: implications for regulatory mechanisms and drug development.Biochemical Society transactions · 2014Review
- Atrial natriuretic factor receptor guanylate cyclase, ANF-RGC, transduces two independent signals, ANF and Ca(2+).Frontiers in molecular neuroscience · 2014Review
- The ANF-RGC gene motif (669)WTAPELL(675) is vital for blood pressure regulation: biochemical mechanism.Biochemistry · 2013Article
- Ca(2+) modulation of ANF-RGC: new signaling paradigm interlocked with blood pressure regulation.Biochemistry · 2012Article
- Guanylyl cyclases A and B are asymmetric dimers that are allosterically activated by ATP binding to the catalytic domain.Science signaling · 2012Article
- A functional screen provides evidence for a conserved, regulatory, juxtamembrane phosphorylation site in guanylyl cyclase a and B.PloS one · 2012Article
- ATP potentiates competitive inhibition of guanylyl cyclase A and B by the staurosporine analog, Gö6976: reciprocal regulation of ATP and GTP binding.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
ANF-RGC is the prototype receptor membrane guanylate cyclase being both the receptor and the signal transducer of the most hypotensive hormones, ANF and BNP. It is a single transmembrane-spanning protein. After binding these hormones at the extracellular domain it at its intracellular domain signals activation of the C-terminal catalytic module and accelerates the production of its second messenger, cyclic GMP, which controls blood pressure, cardiac vasculature, and fluid secretion. ATP is obligatory for the posttransmembrane dynamic events leading to ANF-RGC activation. It functions through the ATP-regulated module, ARM (KHD) domain, of ANF-RGC. In the current over a decade held model "phosphorylation of the KHD is absolutely required for hormone-dependent activation of NPR-A" [Potter, L. R., and Hunter, T. (1998) Mol. Cell. Biol. 18, 2164-2172]. The presented study challenges this concept. It demonstrates that, instead, ATP allosteric modification of ARM is the primary signaling step of ANF-GC activation. In this two-step new dynamic model, ATP in the first step binds ARM. This triggers in it a chain of transduction events, which cause its allosteric modification. The modification partially activates (about 50%) ANF-RGC and, concomitantly, also prepares the ARM for the second successive step. In this second step, ARM is phosphorylated and ANF-RGC achieves additional (∼50%) full catalytic activation. The study defines a new paradigm of the ANF-RGC signaling mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.