May 1, 2000Journal of Biological ChemistryOpen Access

Physical Interactions between Phospholamban and Sarco(endo)plasmic Reticulum Ca2+-ATPases Are Dissociated by Elevated Ca2+, but Not by Phospholamban Phosphorylation, Vanadate, or Thapsigargin, and Are Enhanced by ATP

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Structured PICO

Population

In vitro protein interaction model (phospholamban and fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca2+ ATPase [SERCA1a])

Intervention

Elevated Ca2+, PLN phosphorylation by protein kinase A, ATP, vanadate, and thapsigargin

Comparator

Baseline/control conditions

Outcome

Physical interactions between PLN and SERCA measured by co-immunoprecipitationsurrogate

Elevated Ca2+ dissociates the physical interaction between phospholamban and SERCA, whereas PLN phosphorylation does not, suggesting stable interaction in the Ca2+-free E2 conformation.

Discussion

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Implication

Questions traditional PLN phosphorylation models of SERCA regulation; hypothesis-generating for Ca2+-dependent mechanisms, no practice change yet.

Cite This Study

Asahi et al. (2000) studied this question.

synapsesocial.com/papers/6a834067cd5bc3880318f57a https://doi.org/10.1074/jbc.275.20.15034

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Implication

Questions traditional PLN phosphorylation models of SERCA regulation; hypothesis-generating for Ca2+-dependent mechanisms, no practice change yet.