October 1, 2000Biochemical JournalOpen Access

Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase

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Structured PICO

Population

Co-reconstituted phospholamban (PLB) and affinity-purified Ca-ATPase isolated from skeletal sarcoplasmic reticulum (SR)

Intervention

Phosphorylation of PLB by cAMP-dependent protein kinase (PKA)

Comparator

Unphosphorylated PLB and PLB in the absence of Ca-ATPase

Outcome

Structural interactions, rotational mobility, and tertiary structure changes of PLB and Ca-ATPasesurrogate

Phosphorylation of phospholamban by PKA alters its structural interactions with Ca-ATPase through tertiary rearrangements rather than complete dissociation, modulating calcium transport function.

Authors

SNSewite NegashUniversity of California, Los Angeles QYQing YaoWenzhou Medical University HSHongye SunTianjin University of Technology

Discussion

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Implication

Phosphorylation may modulate cardiac Ca²⁺ handling via retained PLB-SERCA interactions; leaves open functional relevance in disease models.

Cite This Study

Negash et al. (2000) studied this question.

synapsesocial.com/papers/6a82c32ac40fc255ce13414e https://doi.org/10.1042/0264-6021:3510195

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Implication

Phosphorylation may modulate cardiac Ca²⁺ handling via retained PLB-SERCA interactions; leaves open functional relevance in disease models.

Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase

Structured PICO

Discussion

Implication

Cite This Study

Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider