<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Arvanitis, DA</style></author><author><style face="normal" font="default" size="100%">Vafiadaki, E.</style></author><author><style face="normal" font="default" size="100%">Papalouka, V.</style></author><author><style face="normal" font="default" size="100%">Sanoudou, D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Muscle Lim Protein and myosin binding protein C form a complex regulating muscle differentiation</style></title><secondary-title><style face="normal" font="default" size="100%">Biochim Biophys Acta Mol Cell ResBiochim Biophys Acta Mol Cell ResBiochim Biophys Acta Mol Cell Res</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biochimica et biophysica acta. Molecular cell research</style></alt-title><short-title><style face="normal" font="default" size="100%">Biochimica et biophysica acta. Molecular cell researchBiochimica et biophysica acta. Molecular cell research</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Adenosine Triphosphatases/genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Carrier Proteins/*genetics/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Differentiation/*genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Gene Expression Regulation, Developmental</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">LIM Domain Proteins/*genetics/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle Development/*genetics</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle Proteins/*genetics/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle, Striated/growth &amp; development/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscular Diseases/genetics/pathology</style></keyword><keyword><style  face="normal" font="default" size="100%">Myoblasts/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Phosphorylation</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcomeres/genetics</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2017</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Dec</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">12</style></number><volume><style face="normal" font="default" size="100%">1864</style></volume><pages><style face="normal" font="default" size="100%">2308-2321</style></pages><isbn><style face="normal" font="default" size="100%">0167-4889 (Print)0167-4889 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Muscle Lim Protein (MLP) is a protein with multiple functional roles in striated muscle physiology and pathophysiology. Herein, we demonstrate that MLP directly binds to slow, fast, and cardiac myosin-binding protein C (MyBP-C) during myogenesis, as shown by yeast two-hybrid and a range of protein-protein interaction assays. The minimal interacting domains involve MLP inter-LIM and MyBP-C [C4]. The interaction is sensitive to cytosolic Ca(2+) concentrations changes and to MyBP-C phosphorylation by PKA or CaMKII. Confocal microscopy of differentiating myoblasts showed MLP and MyBP-C colocalization during myoblast differentiation. Suppression of the complex formation with recombinant MyBP-C [C4] peptide overexpression, inhibited myoblast differentiation by 65%. Suppression of both MLP and MyBP-C expression in myoblasts by siRNA revealed negative synergistic effects on differentiation. The MLP/MyBP-C complex modulates the actin activated myosin II ATPase activity in vitro, which could interfere with sarcomerogenesis and myofilaments assembly during differentiation. Our data demonstrate a critical role of the MLP/MyBP-C complex during early myoblast differentiation. Its absence in muscles with mutations or aberrant expression of MLP or MyBP-C could be directly implicated in the development of cardiac and skeletal myopathies.</style></abstract><accession-num><style face="normal" font="default" size="100%">28867610</style></accession-num><notes><style face="normal" font="default" size="100%">Arvanitis, Demetrios AVafiadaki, ElizabethPapalouka, VasilikiSanoudou, DespinaengResearch Support, Non-U.S. Gov'tNetherlands2017/09/05 06:00Biochim Biophys Acta Mol Cell Res. 2017 Dec;1864(12):2308-2321. doi: 10.1016/j.bbamcr.2017.08.010. Epub 2017 Sep 1.</style></notes><auth-address><style face="normal" font="default" size="100%">Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, Greece.Molecular Biology Division, Biomedical Research Foundation of the Academy of Athens, Greece; Clinical Genomics and Pharmacogenomics Unit, 4th Department of Internal Medicine, Medical School, National and Kapodistrian University of Athens, Greece. Electronic address: dsanoudou@med.uoa.gr.</style></auth-address></record></records></xml>