ATP allosteric activation of atrial natriuretic factor receptor guanylate cyclase

Duda, Teresa; Yadav, Prem N.; Sharma, Rameshwar K.

doi:10.1111/j.1742-4658.2010.07670.x

Cited by 10 publications

(23 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Half-maximal stimulation was observed at 50 nM staurosporine and the V max of 4.3-fold above basal activity was observed at 1 μM. In accordance with the earlier conclusions (32), these results demonstrate that staurosporine mimics ATP-dependent allostric effect, and that this effect is independent of the phosphorylation of ANF-GC.…”

Section: Resultssupporting

confidence: 92%

“…Staurosporine mimics ATP in allosteric modification of ARM, its effect is independent of phosphorylation and results in partial activation of ANF-RGC (32). …”

Section: Resultsmentioning

confidence: 99%

“…In parallel control experiment, 1 mM AMP-PNP instead of staurosporine was used. AMP-PNP was used as control because previous results have shown that the staurosporine effect on ANF-dependent activity of ANF-RGC is virtually identical to that of AMP-PNP (32). As evident from figure 3B, both staurosporine and AMP-PNP lower the K m of ANF-RGC for GTP.…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Allosteric Modification, the Primary ATP Activation Mechanism of Atrial Natriuretic Factor Receptor Guanylate Cyclase

2011

Self Cite

View full text Add to dashboard Cite

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 post-transmembrane 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 T. Hunter. 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 2-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 ANF-RGC signaling mechanism.

show abstract

Section: Resultssupporting

confidence: 92%

“…Staurosporine mimics ATP in allosteric modification of ARM, its effect is independent of phosphorylation and results in partial activation of ANF-RGC (32). …”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Allosteric Modification, the Primary ATP Activation Mechanism of Atrial Natriuretic Factor Receptor Guanylate Cyclase

2011

Self Cite

View full text Add to dashboard Cite

show abstract

“…4A), which is significantly greater than ATP derived from oxidative phosphorylation. STS inhibits the function of proteins dependent on the coenzyme ATP by invading the active center as an ATP mimetic (Duda et al, 2010). In contrast to a report stating that STS facilitates actin polymerization by directly binding to the ATP-binding cassette of synapsin I (Defranchi et al, 2010), actin-based protrusions were not extended by STS in the absence of ATP (Fig.…”

Section: Discussioncontrasting

confidence: 50%

Staurosporine Induces Formation of Two Types of Extra-Long Cell Protrusions: Actin-Based Filaments and Microtubule-Based Shafts

Kohno

Ninomiya

Kikuchi

et al. 2015

Molecular Pharmacology

View full text Add to dashboard Cite

Staurosporine (STS) has been known as a classic protein kinase C inhibitor and is a broad-spectrum inhibitor targeting over 250 protein kinases. In this study, we observed that STS treatment induced drastic morphologic changes, such as elongation of a very large number of nonbranched, actin-based long cell protrusions that reached up to 30 mm in an hour without caspase activation or PARP cleavage in fibroblasts and epithelial cells. These cell protrusions were elongated not only from the free cell edge but also from the cell-cell junctions. The elongation of STS-dependent protrusions was required for ATP hydrolysis and was dependent on myosin-X and fascin but independent of Cdc42 and VASP. Interestingly, in the presence of an actin polymerization inhibitor, namely, cytochalasin D, latrunculin A, or jasplakinolide, STS treatment induced excess tubulin polymerization, which resulted in the formation of many extra-long microtubule (MT)-based protrusions toward the outside of the cell. The unique MT-based protrusions were thick and linear compared with the STS-induced filaments or stationary filopodia. These protrusions, which were composed of microtubules, have been scarcely observed in cultured non-neuronal cells. Taken together, our findings revealed that STS-sensitive kinases are essential for the maintenance of normal cell morphology, and a common unidentified molecular mechanism is involved in the formation of the following two different types of protrusions: actin-based filaments and MT-based shafts.

show abstract

“…Staurosporine Derivatives Do Not Activate GC-A or GC-BTwo recent studies suggest that staurosporine effectively substitutes for ATP in the activation of GC-A (20,21). Therefore, we tested the ability of Gö6976 and the related compound, staurosporine, to activate GC-A and GC-B (Fig.…”

Section: Gö6976 Is a Competitive Inhibitor Or Gc-a And Gc-b-sub-mentioning

confidence: 99%

ATP Potentiates Competitive Inhibition of Guanylyl Cyclase A and B by the Staurosporine Analog, Gö6976

Robinson

Potter

2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Natriuretic peptides and ATP activate and Gö6976 inhibits guanylyl cyclase (GC)-A and GC-B. Here, the mechanism of inhibition was determined. Gö6976 progressively increased the Michaelis-Menten constant and decreased the Hill coefficient without reducing the maximal velocity of GC-A and GC-B. In the presence of 1 mM ATP, the K i was 1 M for both enzymes. Inhibition of GC-B was minimal in the absence of ATP, and 1 mM ATP increased the inhibition 4-fold. In a reciprocal manner, 10 M Gö6976 increased the potency of ATP for GC-B 4-fold. In contrast to a recent study (Duda, T., Yadav, P., and Sharma, R. K. (2010) FEBS J. 277, 2550 -2553), neither staurosporine nor Gö6976 activated GC-A or GC-B. This is the first study to show that Gö6976 reduces GTP binding and the first demonstration of a competitive inhibitor of a receptor guanylyl cyclase. We conclude that Gö6976 reduces GTP binding to the catalytic site of GC-A and GC-B and that ATP increases the magnitude of the inhibition.

show abstract

ATP allosteric activation of atrial natriuretic factor receptor guanylate cyclase

Cited by 10 publications

References 49 publications

Allosteric Modification, the Primary ATP Activation Mechanism of Atrial Natriuretic Factor Receptor Guanylate Cyclase

Allosteric Modification, the Primary ATP Activation Mechanism of Atrial Natriuretic Factor Receptor Guanylate Cyclase

Staurosporine Induces Formation of Two Types of Extra-Long Cell Protrusions: Actin-Based Filaments and Microtubule-Based Shafts

ATP Potentiates Competitive Inhibition of Guanylyl Cyclase A and B by the Staurosporine Analog, Gö6976

Contact Info

Product

Resources

About