ArticleBiochimica et biophysica acta2013
Molecular basis of the facilitation of the heterooligomeric GIRK1/GIRK4 complex by cAMP dependent protein kinase.
Article in Biochimica et biophysica acta, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 8 citations in OpenAlex.
- Neuronal G protein-gated KAmerican journal of physiology. Cell physiology · 2022Review
- Consequences of somatic mutations of GIRK1 detected in primary malign tumors on expression and function of G-protein activated, inwardly rectifying, KFrontiers in oncology · 2022Article
- Encephalopathy-causing mutations in GβiScience · 2021Article
- The intriguing effect of ethanol and nicotine on acetylcholine-sensitive potassium current IKAch: Insight from a quantitative model.PloS one · 2019Article
- Alteration of gene expression profiling including GPR174 and GNG2 is associated with vasovagal syncope.Pediatric cardiology · 2015Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
G-protein activated inwardly rectifying K(+) channels (GIRKs) of the heterotetrameric GIRK1/GIRK4 composition mediate I(K+ACh) in atrium and are regulated by cAMP dependent protein kinase (PKA). Phosphorylation of GIRK1/GIRK4 complexes promotes the activation of the channel by the G-protein Gβγ-dimer ("heterologous facilitation"). Previously we reported that 3 serines/threonines (S/Ts) within the GIRK1 subunit are phosphorylated by the catalytic subunit of PKA (PKA-cs) in-vitro and are responsible for the acute functional effects exerted by PKA on the homooligomeric GIRK1(F137S) (GIRK1(⁎)) channel. Here we report that homooligomeric GIRK4(WT) and GIRK4(S143T) (GIRK4(⁎)) channels are clearly regulated by PKA phosphorylation. Heterooligomeric channels of the GIRK1(S385CS401CT407C)/GIRK4(WT) composition, where the GIRK1 subunit is devoid of PKA mediated phosphorylation, exhibited reduced but still significant acute effects (reduction during agonist application was ≈49% compared to GIRK1(WT)/GIRK4(WT)). Site directed mutagenesis of truncated cytosolic regions of GIRK4 revealed four serines/threonines (S/Ts) that were heavily phosphorylated by PKA-cs in vitro. Two of them were found to be responsible for the acute effects exerted by PKA in vivo, since the effect of cAMP injection was reduced by ≈99% in homooligomeric GIRK4(⁎T199CS412C) channels. Coexpression of GIRK1(WT)/GIRK4(T199CS412C) reduced the acute effect by ≈65%. Only channels of the GIRK1(S385CS401CT407C)/GIRK4(T199CS412C) composition were practically devoid of PKA mediated effects (reduction by ≈97%), indicating that both subunits contribute to the heterologous facilitation of I(K+ACh).
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