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    Pln phospholamban [ Mus musculus (house mouse) ]

    Gene ID: 18821, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Myofilament Alterations Associated with Human R14del-Phospholamban Cardiomyopathy.

    Myofilament Alterations Associated with Human R14del-Phospholamban Cardiomyopathy.
    Kumar M, Haghighi K, Koch S, Rubinstein J, Stillitano F, Hajjar RJ, Kranias EG, Sadayappan S., Free PMC Article

    02/16/2023
    14-3-3 binding creates a memory of kinase action by stabilizing the modified state of phospholamban.

    14-3-3 binding creates a memory of kinase action by stabilizing the modified state of phospholamban.
    Menzel J, Kownatzki-Danger D, Tokar S, Ballone A, Unthan-Fechner K, Kilisch M, Lenz C, Urlaub H, Mori M, Ottmann C, Shattock MJ, Lehnart SE, Schwappach B.

    10/30/2021
    Phospholamban antisense oligonucleotides improve cardiac function in murine cardiomyopathy.

    Phospholamban antisense oligonucleotides improve cardiac function in murine cardiomyopathy.
    Grote Beverborg N, Später D, Knöll R, Hidalgo A, Yeh ST, Elbeck Z, Silljé HHW, Eijgenraam TR, Siga H, Zurek M, Palmér M, Pehrsson S, Albery T, Bomer N, Hoes MF, Boogerd CJ, Frisk M, van Rooij E, Damle S, Louch WE, Wang QD, Fritsche-Danielson R, Chien KR, Hansson KM, Mullick AE, de Boer RA, van der Meer P., Free PMC Article

    09/25/2021
    Phosphoproteomic analysis identifies phospho-Threonine-17 site of phospholamban important in low molecular weight isoform of fibroblast growth factor 2-induced protection against post-ischemic cardiac dysfunction.

    Phosphoproteomic analysis identifies phospho-Threonine-17 site of phospholamban important in low molecular weight isoform of fibroblast growth factor 2-induced protection against post-ischemic cardiac dysfunction.
    Manning JR, Wijeratne AB, Oloizia BB, Zhang Y, Greis KD, Schultz JEJ., Free PMC Article

    08/14/2021
    The phospholamban p.(Arg14del) pathogenic variant leads to cardiomyopathy with heart failure and is unreponsive to standard heart failure therapy.

    The phospholamban p.(Arg14del) pathogenic variant leads to cardiomyopathy with heart failure and is unreponsive to standard heart failure therapy.
    Eijgenraam TR, Boukens BJ, Boogerd CJ, Schouten EM, van de Kolk CWA, Stege NM, Te Rijdt WP, Hoorntje ET, van der Zwaag PA, van Rooij E, van Tintelen JP, van den Berg MP, van der Meer P, van der Velden J, Silljé HHW, de Boer RA., Free PMC Article

    12/12/2020
    HuR regulates phospholamban expression in isoproterenol-induced cardiac remodelling.

    HuR regulates phospholamban expression in isoproterenol-induced cardiac remodelling.
    Hu H, Jiang M, Cao Y, Zhang Z, Jiang B, Tian F, Feng J, Dou Y, Gorospe M, Zheng M, Zheng L, Yang Z, Wang W., Free PMC Article

    10/24/2020
    the sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA2)-regulating protein phospholamban (PLN) is identified as a physiological SPPL2c substrate.

    The intramembrane protease SPPL2c promotes male germ cell development by cleaving phospholamban.
    Niemeyer J, Mentrup T, Heidasch R, Müller SA, Biswas U, Meyer R, Papadopoulou AA, Dederer V, Haug-Kröper M, Adamski V, Lüllmann-Rauch R, Bergmann M, Mayerhofer A, Saftig P, Wennemuth G, Jessberger R, Fluhrer R, Lichtenthaler SF, Lemberg MK, Schröder B., Free PMC Article

    05/2/2020
    Ablation of phospholamban rescues reperfusion arrhythmias but exacerbates myocardium infarction in hearts with Ca2+/calmodulin kinase II constitutive phosphorylation of ryanodine receptors.

    Ablation of phospholamban rescues reperfusion arrhythmias but exacerbates myocardium infarction in hearts with Ca2+/calmodulin kinase II constitutive phosphorylation of ryanodine receptors.
    Valverde CA, Mazzocchi G, Di Carlo MN, Ciocci Pardo A, Salas N, Ragone MI, Felice JI, Cely-Ortiz A, Consolini AE, Portiansky E, Mosca S, Kranias EG, Wehrens XHT, Mattiazzi A., Free PMC Article

    04/4/2020
    SERCA pumping efficiency (measured as an apparent coupling ratio: Ca(2+) uptake/ATP hydrolysis) was unaffected by PLN deficiency in skeletal muscle. Study lends support to the notion that PLN serves a functionally distinct role from that of sarcolipin in skeletal muscle physiology.

    Phospholamban deficiency does not alter skeletal muscle SERCA pumping efficiency or predispose mice to diet-induced obesity.
    Gamu D, Juracic ES, Fajardo VA, Rietze BA, Tran K, Bombardier E, Tupling AR.

    12/21/2019
    Cardioprotection by PKN1 is associated with reduced CamKIIdelta-dependent phospholamban Thr17 phosphorylation at the SR and therefore may stabilize the coupling of SR Ca2+ handling and contractile function, independent of its kinase activity.

    Loss of Protein Kinase Novel 1 (PKN1) is associated with mild systolic and diastolic contractile dysfunction, increased phospholamban Thr17 phosphorylation, and exacerbated ischaemia-reperfusion injury.
    Francois AA, Obasanjo-Blackshire K, Clark JE, Boguslavskyi A, Holt MR, Parker PJ, Marber MS, Heads RJ., Free PMC Article

    05/25/2019
    Here the show that DWORF has a higher apparent binding affinity for SERCA than PLN and that DWORF overexpression mitigates the contractile dysfunction associated with PLN overexpression, substantiating its role as a potent activator of SERCA.

    The DWORF micropeptide enhances contractility and prevents heart failure in a mouse model of dilated cardiomyopathy.
    Makarewich CA, Munir AZ, Schiattarella GG, Bezprozvannaya S, Raguimova ON, Cho EE, Vidal AH, Robia SL, Bassel-Duby R, Olson EN., Free PMC Article

    02/9/2019
    Oxidative stress upregulates pVHL expression to induce PLN degradation in failing hearts.

    Phospholamban Is Downregulated by pVHL-Mediated Degradation through Oxidative Stress in Failing Heart.
    Yokoe S, Asahi M., Free PMC Article

    07/7/2018
    A single-dose injection of PLN-targeting locked nucleic acid antisense oligonucleotide improved contractility in pressure overload-induced cardiac dysfunction.

    Phospholamban Inhibition by a Single Dose of Locked Nucleic Acid Antisense Oligonucleotide Improves Cardiac Contractility in Pressure Overload-Induced Systolic Dysfunction in Mice.
    Morihara H, Yamamoto T, Oiwa H, Tonegawa K, Tsuchiyama D, Kawakatsu I, Obana M, Maeda M, Mohri T, Obika S, Fujio Y, Nakayama H.

    11/11/2017
    PLN overexpression is associated with severe muscle atrophy and weakness.

    Sarcolipin deletion exacerbates soleus muscle atrophy and weakness in phospholamban overexpressing mice.
    Fajardo VA, Gamu D, Mitchell A, Bloemberg D, Bombardier E, Chambers PJ, Bellissimo C, Quadrilatero J, Tupling AR., Free PMC Article

    09/9/2017
    These data suggest that PLN is, at least partially, oligo-ubiquitinated at Lys(3) and degraded through Ser(16)-phosphorylation-mediated poly-ubiquitination during heart failure.

    Phospholamban degradation is induced by phosphorylation-mediated ubiquitination and inhibited by interaction with cardiac type Sarco(endo)plasmic reticulum Ca(2+)-ATPase.
    Nakagawa T, Yokoe S, Asahi M.

    08/13/2016
    the commercially available overexpressing phospholamban mouse phenotypically resembles human Centronuclear myopathy and could be used as a model to test potential mechanisms and therapeutic strategies.

    Phospholamban overexpression in mice causes a centronuclear myopathy-like phenotype.
    Fajardo VA, Bombardier E, McMillan E, Tran K, Wadsworth BJ, Gamu D, Hopf A, Vigna C, Smith IC, Bellissimo C, Michel RN, Tarnopolsky MA, Quadrilatero J, Tupling AR., Free PMC Article

    04/23/2016
    Cardioprotective effects of H2S are mediated through acGMP/PKG/phospholamban pathway.

    Cardioprotection by H2S engages a cGMP-dependent protein kinase G/phospholamban pathway.
    Bibli SI, Andreadou I, Chatzianastasiou A, Tzimas C, Sanoudou D, Kranias E, Brouckaert P, Coletta C, Szabo C, Kremastinos DT, Iliodromitis EK, Papapetropoulos A., Free PMC Article

    02/13/2016
    PLN pentamers reduce phosphorylation of monomers at baseline and delay monomer phosphorylation upon PKA stimulation leading to increased interaction of PLN monomers with SERCA2a.

    Phospholamban pentamers attenuate PKA-dependent phosphorylation of monomers.
    Wittmann T, Lohse MJ, Schmitt JP.

    11/21/2015
    combined deletion of Phd2 and Phd3 dramatically decreased expression of phospholamban (PLN), resulted in sustained activation of calcium/calmodulin-activated kinase II (CaMKII), and sensitized mice to chronic beta-adrenergic stress-induced myocardial injury

    PHD2/3-dependent hydroxylation tunes cardiac response to β-adrenergic stress via phospholamban.
    Xie L, Pi X, Townley-Tilson WH, Li N, Wehrens XH, Entman ML, Taffet GE, Mishra A, Peng J, Schisler JC, Meissner G, Patterson C., Free PMC Article

    09/26/2015
    the N termini of SLN and PLB influence their respective unique functions

    The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ Transport.
    Sahoo SK, Shaikh SA, Sopariwala DH, Bal NC, Bruhn DS, Kopec W, Khandelia H, Periasamy M., Free PMC Article

    08/22/2015
    CaMKII-dependent increase in PLN phosphorylation during reperfusion opposes rather than contributes to ischemia/reperfusion damage.

    CaMKII-dependent phosphorylation of cardiac ryanodine receptors regulates cell death in cardiac ischemia/reperfusion injury.
    Di Carlo MN, Said M, Ling H, Valverde CA, De Giusti VC, Sommese L, Palomeque J, Aiello EA, Skapura DG, Rinaldi G, Respress JL, Brown JH, Wehrens XH, Salas MA, Mattiazzi A., Free PMC Article

    04/4/2015
    TNAP plays a role in governing the phosphorylation status of phospholamban in the sarcoplasmic reticulum.

    Sex-dependent, zinc-induced dephosphorylation of phospholamban by tissue-nonspecific alkaline phosphatase in the cardiac sarcomere.
    Wang Y, Bishop NM, Taatjes DJ, Narisawa S, Millán JL, Palmer BM., Free PMC Article

    11/8/2014
    SLN and PLN are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2+ in human skeletal muscle.

    Co-expression of SERCA isoforms, phospholamban and sarcolipin in human skeletal muscle fibers.
    Fajardo VA, Bombardier E, Vigna C, Devji T, Bloemberg D, Gamu D, Gramolini AO, Quadrilatero J, Tupling AR., Free PMC Article

    09/20/2014
    Epac1 KO exhibited decreased cardiac contractility with reduced phospholamban (PLN) phosphorylation at serine-16, the major PKA-mediated phosphorylation site.

    Epac1-dependent phospholamban phosphorylation mediates the cardiac response to stresses.
    Okumura S, Fujita T, Cai W, Jin M, Namekata I, Mototani Y, Jin H, Ohnuki Y, Tsuneoka Y, Kurotani R, Suita K, Kawakami Y, Hamaguchi S, Abe T, Kiyonari H, Tsunematsu T, Bai Y, Suzuki S, Hidaka Y, Umemura M, Ichikawa Y, Yokoyama U, Sato M, Ishikawa F, Izumi-Nakaseko H, Adachi-Akahane S, Tanaka H, Ishikawa Y., Free PMC Article

    08/23/2014
    Phospholamban knockout breaks cell-wide propagating spontaneous Ca2+ waves in isolated ventricular myocytes & protects RyR2-mutant mice from stress-induced ventricular tachycardia.

    Phospholamban knockout breaks arrhythmogenic Ca²⁺ waves and suppresses catecholaminergic polymorphic ventricular tachycardia in mice.
    Bai Y, Jones PP, Guo J, Zhong X, Clark RB, Zhou Q, Wang R, Vallmitjana A, Benitez R, Hove-Madsen L, Semeniuk L, Guo A, Song LS, Duff HJ, Chen SR., Free PMC Article

    12/7/2013
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