Evidence for a phosphorylation-induced conformational change in phospholamban cytoplasmic domain by CD analysis.
Phospholamban (PLB), an integral membrane protein of cardiac sarcoplasmic reticulum (SR), is described as the regulator of the Ca(2+)-ATPase pump, via its phosphorylation-dephosphorylation of Ser-16. Recently it has been shown that a direct interaction between the N-terminal hydrophilic domain of PLB and Ca(2+)-ATPase may be one of the mechanisms of regulation. In order to show that this interaction could be modulated by a phosphorylation-induced conformational change in PLB, we ran CD studies on the synthetic peptide PLB(2-33) in its phosphorylated and non-phosphorylated forms, at various pHs, concentrations and in the absence or presence of trifluoroethanol. The results show a clear difference in structure of the phosphorylated and non-phosphorylated peptide.
Terzi
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Laboratoire de Chimie Organique des Substances Naturelles, CNRS URA 31, Strasbourg, France.
Poteur
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L
Trifilieff
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D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000595:Amino Acid Sequence; D002135:Calcium-Binding Proteins / Q000737:chemistry*; D002942:Circular Dichroism; D003593:Cytoplasm / Q000737:chemistry; D008969:Molecular Sequence Data; D010766:Phosphorylation; D011487:Protein Conformation; D012694:Serine / Q000378:metabolism; D000099211:Phospholamban
D000251:Adenosine Triphosphatases; D002135:Calcium-Binding Proteins; D012694:Serine; D000099211:Phospholamban