Synergistic activation of insect cAMP-dependent protein kinase A (type II) by cyclicAMP and cyclicGMP

The high cGMP sensitivity of cAMP-dependent protein kinase A (type II) (PKAII) from invertebrates led to the hypothesis that cGMP directly activates PKAII under physiological conditions. We tested this idea using PKAII holoenzyme purified from the honeybee brain in an assay with short stimulation ti...

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Veröffentlicht in:FEBS letters 2004-10, Vol.576 (1), p.216-220
Hauptverfasser: Leboulle, Gérard, Müller, Uli
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Müller, Uli
description The high cGMP sensitivity of cAMP-dependent protein kinase A (type II) (PKAII) from invertebrates led to the hypothesis that cGMP directly activates PKAII under physiological conditions. We tested this idea using PKAII holoenzyme purified from the honeybee brain in an assay with short stimulation times. In the presence of very low cAMP concentrations, we found a synergistic increase in PKAII activation by physiological cGMP concentrations. Cloning honeybee regulatory subunit RII and phylogenetic comparison of the two cyclic nucleotide-binding sites of RII reveal a high relation of domain A of insect RII with cGMP-binding domains of cGMP-dependent protein kinases.
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subjects Animals
Apis mellifera
Bees - metabolism
Binding Sites
C, catalytic subunit
Computational Biology
Cyclic AMP
Cyclic AMP - metabolism
Cyclic AMP-Dependent Protein Kinase Type II
Cyclic AMP-Dependent Protein Kinases - isolation & purification
Cyclic AMP-Dependent Protein Kinases - metabolism
Cyclic cGMP
Cyclic GMP - metabolism
Enzyme Activation
Insect
Nucleotide-binding site
PBC, phosphate-binding cassette
Phylogeny
PKA, cAMP-dependent protein kinase
PKG, cGMP-dependent protein kinase
Protein kinase A
R, regulatory subunit
Regulatory subunit
title Synergistic activation of insect cAMP-dependent protein kinase A (type II) by cyclicAMP and cyclicGMP
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