March 3, 2006Journal of Biological ChemistryOpen Access

Regulation of Surface Localization of the Small Conductance Ca2+-activated Potassium Channel, Sk2, through Direct Phosphorylation by cAMP-dependent Protein Kinase

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Population

COS7 cells expressing SK2 channel subunits

Comparison

Activation of cyclic AMP-dependent protein… vs Unstimulated cells and wild-type SK2 channel…

Design

Preclinical

Authors

YRYajun RenNanjing Agricultural University LBLyndon Forbes BarnwellBaylor College of Medicine JAJon C. AlexanderUniversity of Florida

Discussion

Member takes

Implication

PKA-dependent SK2 internalization via Ser568-570 is confirmed in vitro; leaves open effects on native cardiac excitability or arrhythmia risk.

Structured PICO

Population

COS7 cells expressing SK2 channel subunits

Intervention

Activation of cyclic AMP-dependent protein kinase (PKA) with forskolin (50 microm) and mutational analysis of SK2 subunits

Comparator

Unstimulated cells and wild-type SK2 channel subunits

Outcome

Surface localization of the SK2 channel subunitsurrogate

PKA phosphorylation at specific serine residues (Ser568, Ser569, Ser570) is necessary for the PKA-mediated decrease in surface expression of SK2 channels.

Cite This Study

Ren et al. (2006) studied this question.

synapsesocial.com/papers/6a8a596be7982ec3bdde8587 https://doi.org/10.1074/jbc.m513125200

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Implication

PKA-dependent SK2 internalization via Ser568-570 is confirmed in vitro; leaves open effects on native cardiac excitability or arrhythmia risk.

Regulation of Surface Localization of the Small Conductance Ca2+-activated Potassium Channel, Sk2, through Direct Phosphorylation by cAMP-dependent Protein Kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Regulation of Surface Localization of the Small Conductance Ca2+-activated Potassium Channel, Sk2, through Direct Phosphorylation by cAMP-dependent Protein Kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider