August 20, 2003Biochemistry

Phosphorylation by cAMP-Dependent Protein Kinase Modulates the Structural Coupling between the Transmembrane and Cytosolic Domains of Phospholamban

View Full Paper

Ask AI

Bookmark

Population

Engineered phospholamban reconstituted in membrane vesicles made from extracted sarcoplasmic reticulum…

Comparison

Phosphorylation of Ser by cAMP-dependent protein… vs Unphosphorylated PLB

Design

Preclinical

Authors

JLJinhui LiJinan University DBDiana J. BigelowUniversity of Pennsylvania TSThomas C. SquierWestern University of Health Sciences

Discussion

Member takes

Implication

May stabilize phospholamban hinge to relieve SERCA inhibition; leaves open translation to human cardiac therapies.

Structured PICO

Population

Engineered phospholamban (PLB) reconstituted in membrane vesicles made from extracted sarcoplasmic reticulum membrane lipids

Intervention

Phosphorylation of Ser(16) by cAMP-dependent protein kinase (PKA)

Comparator

Unphosphorylated PLB

Outcome

Spatial separation and conformational heterogeneity between the transmembrane and cytosolic domains measured by fluorescence resonance energy transfer (FRET)surrogate

Phosphorylation of phospholamban by PKA stabilizes its hinge region, acting as a conformational switch to relieve inhibition of the Ca-ATPase.

Cite This Study

Li et al. (2003) studied this question.

synapsesocial.com/papers/6a82c32ac40fc255ce134144 https://doi.org/10.1021/bi034708c

View Full Paper

Ask AI

Bookmark

Phosphorylation by cAMP-Dependent Protein Kinase Modulates the Structural Coupling between the Transmembrane and Cytosolic Domains of Phospholamban

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Phosphorylation by cAMP-Dependent Protein Kinase Modulates the Structural Coupling between the Transmembrane and Cytosolic Domains of Phospholamban

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider