Effects of phospholamban phosphorylation catalyzed by adenosine 3′:5′-monophosphate- and calmodulin-dependent protein kinases on calcium transport ATPase of cardiac sarcoplasmic reticulum☆
References (32)
- et al.
The Ca2+-pumping ATPase of heart sarcolemma. Characterization, calmodulin dependence, and partial purification
J Biol Chem
(1981) - et al.
Phosphodiesterase protein activator stimulates cardiac transport in cardiac microsomal preparations enriched in sarcoplasmic reticulum
Biochem Biophys Res Commun
(1978) - et al.
Calmodulin-mediated regulation of calcium transport and (Ca2+ Mg2+)-activated ATPase activity in isolated cardiac sarcoplasmic reticulum
J Biol Chem
(1982) - et al.
Adenosine 3′:5′-monophosphate-dependent protein kinase-catalyzed phosphorylation reaction and its relationships to calcium transport in cardiac sarcoplasmic reticulum
J Biol Chem
(1974) - et al.
Phosphorylation of low molecular weight proteins in purified preparations of rat heart sarcolemma and sarcoplasmic reticulum
Biochim Biophys Acta
(1980) - et al.
Phospholamban phosphorylation in the perfused rat heart is not solely dependent on β-adrenergic stimulation
FEBS Lett
(1980) - et al.
Protein measurement with the folin phenol reagent
J Biol Chem
(1951) - et al.
The rate of calcium uptake in sarcoplasmic reticulum of cardiac muscle and skeletal muscle. Effects of cyclic AMP-dependent protein kinase and phosphorylase b kinase
Biochim Biophys Acta
(1976) - et al.
Phosphorylation of a 22 000-dalton component of the cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase
J Biol Chem
(1975) - et al.
The stimulation of calcium transport in cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase
J Biol Chem
(1974)
Mechanism of the stimulation of Ca2+-dependent ATPase of cardiac sarcoplasmic reticulum by adenosine 3′:5′-monophosphate-dependent protein kinase. Role of the 22 000-dalton protein
J Biol Chem
Transient state kinetic studies of Ca2+-dependent ATPase and calcium transport by cardiac sarcoplasmic reticulum. Effect of cyclic AMP-dependent protein kinase-catalyzed phosphorylation of phospholamban
J Biol Chem
A quench-flow kinetic investigation of calcium ion accumulation by isolated cardiac sarcoplasmic reticulum. Dependence of initial velocity on free calcium ion concentration and influence of preincubation with a protein kinase, MgATP and cyclic AMP
Biochim Biophys Acta
Cyclic AMP stimulation of membrane phosphorylation and Ca2+-activated, Mg2+ dependent ATPase in cardiac sarcoplasmic reticulum
Biochim Biophys Acta
Identification of an activator protein for myosin light chain kinase as the Ca2+-dependent modulator protein
J Biol Chem
Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase
Circ Res
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Association with SERCA2a directs phospholamban trafficking to sarcoplasmic reticulum from a nuclear envelope pool
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2019, Journal of Molecular BiologyA pyridone derivative activates SERCA2a by attenuating the inhibitory effect of phospholamban
2017, European Journal of PharmacologyMolecular dynamics simulations of biological membranes and membrane proteins using enhanced conformational sampling algorithms
2016, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :How PLN interacts with SERCA to regulate the ion uptake is the central question, yet it remains unresolved. Biochemical experiments showed that phosphorylation of PLN at Ser16 by cAMP-dependent protein kinase [211] or at Thr17 by Ca2+/calmodulin-dependent kinase relieves the inhibition [212]. However, molecular mechanisms underlying the regulation remain elusive.
A cell-penetrating phospholamban-specific RNA aptamer enhances Ca<sup>2+</sup> transients and contractile function in cardiomyocytes
2014, Journal of Molecular and Cellular CardiologyCitation Excerpt :The reaction was initiated by the addition of ATP and stopped by that of 170 μl of a solution containing 0.3 mM 2,4-dinitrophenylhydrazine and 0.35 M HCl. The Ca2 +-dependent ATPase activity was then determined as described previously [25]. Free Ca2 + concentrations were calculated with the use of the WEBMAXC program (http://maxchelator.stanford.edu).
Synthetic phosphopeptides enable quantitation of the content and function of the four phosphorylation states of phospholamban in cardiac muscle
2014, Journal of Biological Chemistry
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Supported by research grants from the Ministry of Education, Science and Culture of Japan, and a Grant-in-Aid from Muscular Dystrophy Association of America.