Schrul, Bianca

[["dc.bibliographiccitation.firstpage","473"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","483"],["dc.bibliographiccitation.volume","126"],["dc.contributor.author","Powis, Katie"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Tienson, Heather"],["dc.contributor.author","Gostimskaya, Irina"],["dc.contributor.author","Breker, Michal"],["dc.contributor.author","High, Stephen"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Jakob, Ursula"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:48:18Z"],["dc.date.available","2017-09-07T11:48:18Z"],["dc.date.issued","2013"],["dc.description.abstract","The endomembrane system of yeast contains different tail-anchored proteins that are post-translationally targeted to membranes via their C-terminal transmembrane domain. This hydrophobic segment could be hazardous in the cytosol if membrane insertion fails, resulting in the need for energy-dependent chaperoning and the degradation of aggregated tail-anchored proteins. A cascade of GET proteins cooperates in a conserved pathway to accept newly synthesized tail-anchored proteins from ribosomes and guide them to a receptor at the endoplasmic reticulum, where membrane integration takes place. It is, however, unclear how the GET system reacts to conditions of energy depletion that might prevent membrane insertion and hence lead to the accumulation of hydrophobic proteins in the cytosol. Here we show that the ATPase Get3, which accommodates the hydrophobic tail anchor of clients, has a dual function: promoting tail-anchored protein insertion when glucose is abundant and serving as an ATP-independent holdase chaperone during energy depletion. Like the generic chaperones Hsp42, Ssa2, Sis1 and Hsp104, we found that Get3 moves reversibly to deposition sites for protein aggregates, hence supporting the sequestration of tail-anchored proteins under conditions that prevent tail-anchored protein insertion. Our findings support a ubiquitous role for the cytosolic GET complex as a triaging platform involved in cellular proteostasis."],["dc.identifier.doi","10.1242/jcs.112151"],["dc.identifier.gro","3142404"],["dc.identifier.isi","000316945600011"],["dc.identifier.pmid","23203805"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10654"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7908"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9533"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2106"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","2119"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Brandenburg, Sören"],["dc.contributor.author","Uchida, Keita"],["dc.contributor.author","Zhang, Haixia"],["dc.contributor.author","Lin, Yu-Wen"],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Sulkin, Matthew S."],["dc.contributor.author","Efimov, Igor R."],["dc.contributor.author","Nichols, Colin G."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:46:16Z"],["dc.date.available","2017-09-07T11:46:16Z"],["dc.date.issued","2014"],["dc.description.abstract","The copy number of membrane proteins at the cell surface is tightly regulated. Many ion channels and receptors present retrieval motifs to COPI vesicle coats and are retained in the early secretory pathway. In some cases, the interaction with COPI is prevented by binding to 14-3- 3 proteins. However, the functional significance of this antagonism between COPI and 14-3-3 in terminally differentiated cells is unknown. Here, we show that ATP-sensitive K+ (K-ATP) channels, which are composed of Kir6.2 and SUR1 subunits, are stalled in the Golgi complex of ventricular, but not atrial, cardiomyocytes. Upon sustained beta-adrenergic stimulation, which leads to activation of protein kinase A (PKA), SUR1-containing channels reach the plasma membrane of ventricular cells. We show that PKA-dependent phosphorylation of the C-terminus of Kir6.2 decreases binding to COPI and, thereby, silences the arginine-based retrieval signal. Thus, activation of the sympathetic nervous system releases this population of KATP channels from storage in the Golgi and, hence, might facilitate the adaptive response to metabolic challenges."],["dc.identifier.doi","10.1242/jcs.141440"],["dc.identifier.gro","3142132"],["dc.identifier.isi","000335814800021"],["dc.identifier.pmid","24569881"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10660"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4900"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/3"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A05: Molekulares Imaging von kardialen Calcium-Freisetzungsdomänen"],["dc.relation","SFB 1002 | A07:Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation.eissn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.relation.workinggroup","RG Brandenburg"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Tuning the electrical properties of the heart by differential trafficking of K-ATP ion channel complexes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e39703"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Wolf, Wendelin"],["dc.contributor.author","Kilic, Annett"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Lorenz, Holger"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Seedorf, Matthias"],["dc.date.accessioned","2017-09-07T11:48:50Z"],["dc.date.available","2017-09-07T11:48:50Z"],["dc.date.issued","2012"],["dc.description.abstract","The endoplasmic reticulum (ER) forms contacts with the plasma membrane. These contacts are known to function in non-vesicular lipid transport and signaling. Ist2 resides in specific domains of the ER in Saccharomyces cerevisiae where it binds phosphoinositide lipids at the cytosolic face of the plasma membrane. Here, we report that Ist2 recruits domains of the yeast ER to the plasma membrane. Ist2 determines the amount of cortical ER present and the distance between the ER and the plasma membrane. Deletion of IST2 resulted in an increased distance between ER and plasma membrane and allowed access of ribosomes to the space between the two membranes. Cells that overexpress Ist2 showed an association of the nucleus with the plasma membrane. The morphology of the ER and yeast growth were sensitive to the abundance of Ist2. Moreover, Ist2-dependent effects on cytosolic pH and genetic interactions link Ist2 to the activity of the H+ pump Pma1 in the plasma membrane during cellular adaptation to the growth phase of the culture. Consistently we found a partial colocalization of Ist2-containing cortical ER and Pma1-containing domains of the plasma membrane. Hence Ist2 may be critically positioned in domains that couple functions of the ER and the plasma membrane."],["dc.identifier.doi","10.1371/journal.pone.0039703"],["dc.identifier.gro","3142496"],["dc.identifier.isi","000306354700017"],["dc.identifier.pmid","22808051"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7867"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8854"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [SE 811/5-2]"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Yeast Ist2 Recruits the Endoplasmic Reticulum to the Plasma Membrane and Creates a Ribosome-Free Membrane Microcompartment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]