Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)

Anastasia Pyriochou; Antonis Tsarbopoulos; Andreas Papapetropoulos

Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)

Anastasia Pyriochou
, Antonis Tsarbopoulos
, Andreas Papapetropoulos

Surgery

Research output: Contribution to journal › Article › peer-review

Abstract

Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.

Original language	English (US)
Pages (from-to)	311-313
Number of pages	3
Journal	Review of Clinical Pharmacology and Pharmacokinetics, International Edition
Volume	20
Issue number	2
State	Published - 2006

Keywords

Phosphorylation
Soluble guanylyl cyclase
cAMP-dependent protein kinase
cGMP

ASJC Scopus subject areas

Pharmacology (medical)

Cite this

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abstract = "Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.",

keywords = "Phosphorylation, Soluble guanylyl cyclase, cAMP-dependent protein kinase, cGMP",

author = "Anastasia Pyriochou and Antonis Tsarbopoulos and Andreas Papapetropoulos",

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T1 - Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)

AU - Pyriochou, Anastasia

AU - Tsarbopoulos, Antonis

AU - Papapetropoulos, Andreas

PY - 2006

Y1 - 2006

N2 - Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.

AB - Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.

KW - Phosphorylation

KW - Soluble guanylyl cyclase

KW - cAMP-dependent protein kinase

KW - cGMP

UR - https://www.scopus.com/pages/publications/33744462883

UR - https://www.scopus.com/pages/publications/33744462883#tab=citedBy

M3 - Article

AN - SCOPUS:33744462883

SN - 1011-6583

VL - 20

SP - 311

EP - 313

JO - Review of Clinical Pharmacology and Pharmacokinetics, International Edition

JF - Review of Clinical Pharmacology and Pharmacokinetics, International Edition

IS - 2

ER -

Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)

Abstract

Keywords

ASJC Scopus subject areas

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