A hallmark of phospholamban functional divergence is located in the N-terminal phosphorylation domain

scientific article published on 28 February 2020

A hallmark of phospholamban functional divergence is located in the N-terminal phosphorylation domain is …
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scholarly articleQ13442814

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P356DOI10.1016/J.CSBJ.2020.02.016
P932PMC publication ID7114604
P698PubMed publication ID32257054

P50authorRodrigo Aguayo-OrtizQ64683190
P2093author name stringJoseph M Autry
Eli Fernández-de Gortari
L Michel Espinoza-Fonseca
P2860cites workStructure and orientation of sarcolipin in lipid environmentsQ24292113
Effects of phospholamban transmembrane mutants on the calcium affinity, maximal activity, and cooperativity of the sarcoplasmic reticulum calcium pumpQ24309928
Modulation of cardiac contractility by the phospholamban/SERCA2a regulatomeQ24337593
Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulumQ24533577
Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholambanQ24678050
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolutionQ27625023
The Structural Basis for Phospholamban Inhibition of the Calcium Pump in Sarcoplasmic ReticulumQ27679847
SERCA mutant E309Q binds two Ca2+ions but adopts a catalytically incompetent conformationQ27680675
Crystal structures of the calcium pump and sarcolipin in the Mg2+-bound E1 stateQ27684107
The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasmQ27684110
Scalable molecular dynamics with NAMDQ27860718
Update of the CHARMM all-atom additive force field for lipids: validation on six lipid typesQ29616710
Functional reconstitution of recombinant phospholamban with rabbit skeletal Ca(2+)-ATPaseQ30464872
Sarcolipin is a newly identified regulator of muscle-based thermogenesis in mammals.Q30540446
Phosphorylation-induced structural changes in smooth muscle myosin regulatory light chainQ33929417
Atomic-level mechanisms for phospholamban regulation of the calcium pump.Q35333572
Sarcolipin Is a Key Determinant of the Basal Metabolic Rate, and Its Overexpression Enhances Energy Expenditure and Resistance against Diet-induced Obesity.Q35536274
The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ TransportQ35662355
Optimization of the additive CHARMM all-atom protein force field targeting improved sampling of the backbone φ, ψ and side-chain χ(1) and χ(2) dihedral anglesQ36546184
Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tailQ36708601
Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPaseQ37232028
Differential expression of sarcolipin protein during muscle development and cardiac pathophysiologyQ37252432
Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholambanQ37255989
The sarcoplasmic Ca2+-ATPase: design of a perfect chemi-osmotic pumpQ37784543
Thermodynamic and structural basis of phosphorylation-induced disorder-to-order transition in the regulatory light chain of smooth muscle myosin.Q40709998
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.Q40880128
Phospholamban domain Ib mutations influence functional interactions with the Ca2+-ATPase isoform of cardiac sarcoplasmic reticulumQ41035597
Increased Reliance on Muscle-based Thermogenesis upon Acute Minimization of Brown Adipose Tissue FunctionQ41045820
Phospholamban domain I/cytochrome b5 transmembrane sequence chimeras do not inhibit SERCA2aQ41047973
Phospholamban inhibitory function is activated by depolymerizationQ41105112
Phospholamban regulates the Ca2+-ATPase through intramembrane interactionsQ41168796
Sarcolipin and phospholamban mRNA and protein expression in cardiac and skeletal muscle of different species.Q41768288
Sarcolipin and phospholamban inhibit the calcium pump by populating a similar metal ion-free intermediate state.Q41834129
Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain.Q42675569
Sarcolipin Promotes Uncoupling of the SERCA Ca2+ Pump by Inducing a Structural Rearrangement in the Energy-Transduction DomainQ42943217
Sarcolipin, the shorter homologue of phospholamban, forms oligomeric structures in detergent micelles and in liposomesQ43645352
On the role of electrostatic interactions in the design of protein-protein interfacesQ44021056
Ablation of sarcolipin decreases the energy requirements for Ca2+ transport by sarco(endo)plasmic reticulum Ca2+-ATPases in resting skeletal muscleQ44123306
Ca2+ occlusion and gating function of Glu309 in the ADP-fluoroaluminate analog of the Ca2+-ATPase phosphoenzyme intermediateQ44901190
Protein-phospholipid interplay revealed with crystals of a calcium pump.Q51022558
Improved Treatment of Ligands and Coupling Effects in Empirical Calculation and Rationalization of pKa Values.Q51550011
The presence of sarcolipin results in increased heat production by Ca(2+)-ATPase.Q51932184
Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading.Q52310162
A solid-state NMR study of the phospholamban transmembrane domain: local structure and interactions with Ca(2+)-ATPase.Q52541181
Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box sizeQ56797790
PROPKA3: Consistent Treatment of Internal and Surface Residues in Empirical pKa PredictionsQ57129760
Regulatory Role of Phospholamban in the Efficiency of Cardiac Sarcoplasmic Reticulum Ca2+Transport†Q62083031
Molecular mechanism of regulation of Ca2+ pump ATPase by phospholamban in cardiac sarcoplasmic reticulum. Effects of synthetic phospholamban peptides on Ca2+ pump ATPaseQ68052326
Residues 2-25 of phospholamban are insufficient to inhibit Ca2+ transport ATPase of cardiac sarcoplasmic reticulumQ70745212
Defining the molecular components of calcium transport regulation in a reconstituted membrane systemQ73267227
Synthetic null-cysteine phospholamban analogue and the corresponding transmembrane domain inhibit the Ca-ATPaseQ74290669
Microsecond Molecular Simulations Reveal a Transient Proton Pathway in the Calcium PumpQ85264779
Correlation Coefficients: Appropriate Use and InterpretationQ87882653
Redistribution of SERCA calcium pump conformers during intracellular calcium signalingQ88683670
Structural basis for relief of phospholamban-mediated inhibition of the sarcoplasmic reticulum Ca2+-ATPase at saturating Ca2+ conditionsQ89206165
Phospholamban deficiency does not alter skeletal muscle SERCA pumping efficiency or predispose mice to diet-induced obesityQ90849426
The Phospholamban Pentamer Alters Function of the Sarcoplasmic Reticulum Calcium Pump SERCAQ91321387
Thermodynamics of Cation Binding to the Sarcoendoplasmic Reticulum Calcium ATPase Pump and Impacts on Enzyme FunctionQ91929376
Newly Discovered Micropeptide Regulators of SERCA Form Oligomers but Bind to the Pump as MonomersQ92869535
P304page(s)705-713
P577publication date2020-02-28
P1433published inComputational and Structural Biotechnology JournalQ19865804
P1476titleA hallmark of phospholamban functional divergence is located in the N-terminal phosphorylation domain
P478volume18

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