Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes.

@article{Hagemann2000FrequencyencodingTP,
  title={Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes.},
  author={Dirk Hagemann and Meike Kuschel and Takashi Kuramochi and Wuqiang Zhu and Heping Cheng and Rui Ping Xiao},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 29},
  pages={22532-6}
}
Both Ser(16) and Thr(17) of phospholamban (PLB) are phosphorylated, respectively, by cAMP-dependent protein kinase (PKA) and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). PLB phosphorylation relieves cardiac sarcoplasmic reticulum Ca(2+) pump from inhibition by PLB. Previous studies have suggested that phosphorylation of Ser(16) by PKA is a prerequisite for Thr(17) phosphorylation by CaMKII and is essential to the relaxant effect of beta-adrenergic stimulation. To determine the role… CONTINUE READING

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Both Ser(16 ) and Thr(17 ) of phospholamban ( PLB ) are phosphorylated , respectively , by cAMP - dependent protein kinase ( PKA ) and Ca(2+)/calmodulin - dependent protein kinase II ( CaMKII ) .
Both Ser(16 ) and Thr(17 ) of phospholamban ( PLB ) are phosphorylated , respectively , by cAMP - dependent protein kinase ( PKA ) and Ca(2+)/calmodulin - dependent protein kinase II ( CaMKII ) .
Both Ser(16 ) and Thr(17 ) of phospholamban ( PLB ) are phosphorylated , respectively , by cAMP - dependent protein kinase ( PKA ) and Ca(2+)/calmodulin - dependent protein kinase II ( CaMKII ) .
Thus , we conclude that in intact cardiac myocytes , phosphorylation of PLB at Thr(17 ) occurs in the absence of prior Ser(16 ) phosphorylation , and that frequencydependent Thr(17 ) PLB phosphorylation may provide an intrinsic mechanism for cardiac myocytes to adapt to a sudden change of heart rate .
Thus , we conclude that in intact cardiac myocytes , phosphorylation of PLB at Thr(17 ) occurs in the absence of prior Ser(16 ) phosphorylation , and that frequencydependent Thr(17 ) PLB phosphorylation may provide an intrinsic mechanism for cardiac myocytes to adapt to a sudden change of heart rate .
Thus , we conclude that in intact cardiac myocytes , phosphorylation of PLB at Thr(17 ) occurs in the absence of prior Ser(16 ) phosphorylation , and that frequencydependent Thr(17 ) PLB phosphorylation may provide an intrinsic mechanism for cardiac myocytes to adapt to a sudden change of heart rate .
Thus , we conclude that in intact cardiac myocytes , phosphorylation of PLB at Thr(17 ) occurs in the absence of prior Ser(16 ) phosphorylation , and that frequencydependent Thr(17 ) PLB phosphorylation may provide an intrinsic mechanism for cardiac myocytes to adapt to a sudden change of heart rate .
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