Ryanodine receptor phosphorylation at Serine 2030, 2808 and 2814 in rat cardiomyocytes

Sabine Huke, Donald M Bers

Research output: Contribution to journalArticle

76 Scopus citations

Abstract

The cardiac ryanodine receptor (RyR) controls Ca2+ release from the sarcoplasmic reticulum (SR) during excitation-contraction coupling. Three phosphorylation sites have been identified: Serine-(S)2808, S2814 and recently S2030. We measured phosphorylation with at least two different antibodies per site and demonstrate that for S2808 results were highly antibody-dependent and two out of three S2808 antibodies did not accurately report phosphorylation level. The RyR was substantially phosphorylated in quiescent rat cardiomyocytes at S2808 and less so at S2814, but appeared to be unphosphorylated at S2030. Basal phosphorylation at S2808/S2814 was maintained by a Ca2+ dependent kinase other than Ca2+/Calmodulin-dependent kinase (CaMKII). During stimulation with Isoproterenol S2808 was phosphorylated by protein kinase A (PKA) and S2814 was phosphorylated by CaMKII. Phosphatase 1 appears to be the main phosphatase dephosphorylating S2808/S2814, but phosphatase 2a may also dephosphorylate S2814. RyR phosphorylation is complex, but important in understanding RyR functional modulation.

Original languageEnglish (US)
Pages (from-to)80-85
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume376
Issue number1
DOIs
StatePublished - Nov 7 2008

Keywords

  • Calmodulin-dependent kinase type II (CaMKII)
  • Phosphatase 1 (PP1)
  • Phosphatase 2a (PP2a)
  • Protein kinase A (PKA)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Fingerprint Dive into the research topics of 'Ryanodine receptor phosphorylation at Serine 2030, 2808 and 2814 in rat cardiomyocytes'. Together they form a unique fingerprint.

  • Cite this