Wagner, Eva

[["dc.bibliographiccitation.firstpage","429a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","112"],["dc.contributor.author","Gotthardt, Michael"],["dc.contributor.author","Rudolph, Franziska"],["dc.contributor.author","Huettemeister, Judith"],["dc.contributor.author","da Sliva Lopes, Katharina"],["dc.contributor.author","Yu, Lily"],["dc.contributor.author","Bergmann, Nora"],["dc.contributor.author","Fink, Claudia"],["dc.contributor.author","Wagner, Eva"],["dc.contributor.author","Lehnart, Stephan"],["dc.contributor.author","Gregorio, Carol"],["dc.date.accessioned","2020-12-10T14:22:43Z"],["dc.date.available","2020-12-10T14:22:43Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.bpj.2016.11.2293"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71704"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","From Ribosome to Sarcomere - Titin Dynamics in Striated Muscle Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3999"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","4015"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Brandenburg, Sören"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Williams, George S. B."],["dc.contributor.author","Gusev, Konstantin"],["dc.contributor.author","Wagner, Eva"],["dc.contributor.author","Rog-Zielinska, Eva A."],["dc.contributor.author","Hebisch, Elke"],["dc.contributor.author","Dura, Miroslav"],["dc.contributor.author","Didié, Michael"],["dc.contributor.author","Gotthardt, Michael"],["dc.contributor.author","Nikolaev, Viacheslav O."],["dc.contributor.author","Kohl, Peter"],["dc.contributor.author","Ward, Christopher W."],["dc.contributor.author","Lederer, W. Jonathan"],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Hasenfuß, Gerd"],["dc.date.accessioned","2020-12-10T18:38:18Z"],["dc.date.available","2020-12-10T18:38:18Z"],["dc.date.issued","2016"],["dc.description.abstract","The canonical atrial myocyte (AM) is characterized by sparse transverse tubule (TT) invaginations and slow intracellular Ca2+ propagation but exhibits rapid contractile activation that is susceptible to loss of function during hypertrophic remodeling. Here, we have identified a membrane structure and Ca2+-signaling complex that may enhance the speed of atrial contraction independently of phospholamban regulation. This axial couplon was observed in human and mouse atria and is composed of voluminous axial tubules (ATs) with extensive junctions to the sarcoplasmic reticulum (SR) that include ryanodine receptor 2 (RyR2) clusters. In mouse AM, AT structures triggered Ca2+ release from the SR approximately 2 times faster at the AM center than at the surface. Rapid Ca2+ release correlated with colocalization of highly phosphorylated RyR2 clusters at AT-SR junctions and earlier, more rapid shortening of central sarcomeres. In contrast, mice expressing phosphorylation-incompetent RyR2 displayed depressed AM sarcomere shortening and reduced in vivo atrial contractile function. Moreover, left atrial hypertrophy led to AT proliferation, with a marked increase in the highly phosphorylated RyR2-pS2808 cluster fraction, thereby maintaining cytosolic Ca2+ signaling despite decreases in RyR2 cluster density and RyR2 protein expression. AT couplon \"super-hubs\" thus underlie faster excitation-contraction coupling in health as well as hypertrophic compensatory adaptation and represent a structural and metabolic mechanism that may contribute to contractile dysfunction and arrhythmias."],["dc.identifier.doi","10.1172/JCI88241"],["dc.identifier.gro","3141610"],["dc.identifier.isi","000384703300035"],["dc.identifier.pmid","27643434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77268"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/151"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A01: cAMP- und cGMP- Mikrodomänen bei Herzhypertrophie und Insuffizienz"],["dc.relation","SFB 1002 | A09: Lokale molekulare Nanodomänen-Regulation der kardialen Ryanodin-Rezeptor-Funktion"],["dc.relation","SFB 1002 | S01: In vivo und in vitro Krankheitsmodelle"],["dc.relation","SFB 1002 | S02: Hochauflösende Fluoreszenzmikroskopie und integrative Datenanalyse"],["dc.relation","SFB 1002 | Z: Zentrale Organisation und Verwaltung"],["dc.relation.eissn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.relation.workinggroup","RG Brandenburg"],["dc.relation.workinggroup","RG Hasenfuß (Transition zur Herzinsuffizienz)"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Nikolaev (Cardiovascular Research Center)"],["dc.title","Axial tubule junctions control rapid calcium signaling in atria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","25126"],["dc.bibliographiccitation.issue","50"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","25136"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Rudolph, Franziska"],["dc.contributor.author","Hüttemeister, Judith"],["dc.contributor.author","da Silva Lopes, Katharina"],["dc.contributor.author","Jüttner, René"],["dc.contributor.author","Yu, Lily"],["dc.contributor.author","Bergmann, Nora"],["dc.contributor.author","Friedrich, Dhana"],["dc.contributor.author","Preibisch, Stephan"],["dc.contributor.author","Wagner, Eva"],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Gregorio, Carol C."],["dc.contributor.author","Gotthardt, Michael"],["dc.date.accessioned","2020-04-02T15:03:38Z"],["dc.date.available","2020-04-02T15:03:38Z"],["dc.date.issued","2019"],["dc.description.abstract","Cardiac protein homeostasis, sarcomere assembly, and integration of titin as the sarcomeric backbone are tightly regulated to facilitate adaptation and repair. Very little is known on how the >3-MDa titin protein is synthesized, moved, inserted into sarcomeres, detached, and degraded. Here, we generated a bifluorescently labeled knockin mouse to simultaneously visualize both ends of the molecule and follow titin's life cycle in vivo. We find titin mRNA, protein synthesis and degradation compartmentalized toward the Z-disk in adult, but not embryonic cardiomyocytes. Originating at the Z-disk, titin contributes to a soluble protein pool (>15% of total titin) before it is integrated into the sarcomere lattice. Titin integration, disintegration, and reintegration are stochastic and do not proceed sequentially from Z-disk to M-band, as suggested previously. Exchange between soluble and integrated titin depends on titin protein composition and differs between individual cardiomyocytes. Thus, titin dynamics facilitate embryonic vs. adult sarcomere remodeling with implications for cardiac development and disease."],["dc.identifier.doi","10.1073/pnas.1904385116"],["dc.identifier.pmid","31757849"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63571"],["dc.language.iso","en"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.relation.issn","1091-6490"],["dc.title","Resolving titin's lifecycle and the spatial organization of protein turnover in mouse cardiomyocytes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]