What question did this study set out to answer?

To identify crucial sites in phospholamban responsible for interacting with the Ca(2+)-ATPase.

January 1, 1994Journal of Biological ChemistryOpen Access

Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.

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Population

HEK-293 cells co-expressing the cardiac/slow-twitch muscle Ca-ATPase isozyme and a series of phospholamban…

Comparison

Mutation of amino acid residues in the… vs Wild-type phospholamban or mutations in other…

Design

Preclinical

Authors

TTToshihiko ToyofukuIhara Chemical Industry (Japan)KKKazimierz KurzydlowskiUniversity of Toronto MTMichihiko TadaUniversity of Vermont

Discussion

Member takes

Implication

The 1A domain of phospholamban may be a key modulator of SERCA2a; leaves open whether this informs therapies in heart failure.

Key Points

To identify crucial sites in phospholamban responsible for interacting with the Ca(2+)-ATPase.
Co-expressed phospholamban mutants with cardiac Ca(2+)-ATPase SERCA2a in HEK-293 cells.
Focused on mutations in the cytoplasmic and transmembrane regions of phospholamban.
Analyzed effects on Ca2+ transport inhibition by mutating specific residues.
Mutations in the cytoplasmic 1A domain resulted in loss of phospholamban's inhibitory effect on Ca2+ transport.
Residues Lys3, Arg9, Arg13, Arg14, Glu2, Val4, Leu7, Ala11, Ile12, Ala15, and Ile18 were essential for inhibition.
Mutations outside the 1A domain did not affect phospholamban's inhibitory effects.

Structured PICO

Population

HEK-293 cells co-expressing the cardiac/slow-twitch muscle Ca(2+)-ATPase isozyme (SERCA2a) and a series of phospholamban mutants

Intervention

Mutation of amino acid residues in the cytoplasmic and transmembrane regions of phospholamban

Comparator

Wild-type phospholamban or mutations in other domains (e.g., 1B domain or transmembrane domain)

Outcome

Inhibitory effect of phospholamban on Ca2+ transport by the Ca(2+)-ATPasesurrogate

The cytoplasmic 1A domain of phospholamban (amino acids Glu2 to Ile18) is essential for its functional association with and inhibition of the cardiac sarcoplasmic reticulum Ca(2+)-ATPase.

Cite This Study

Toyofuku et al. (1994) studied this question.

synapsesocial.com/papers/6a720ca75d37378ac1defc0d https://doi.org/10.1016/s0021-9258(17)42051-5

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Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

Amino acids Glu2 to Ile18 in the cytoplasmic domain of phospholamban are essential for functional association with the Ca(2+)-ATPase of sarcoplasmic reticulum.

Discussion

Member takes

Implication

Key Points

Structured PICO

Cite This Study

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