Arakel, Eric Clement

[["dc.bibliographiccitation.artnumber","jcs209890"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2020-12-10T18:41:52Z"],["dc.date.available","2020-12-10T18:41:52Z"],["dc.date.issued","2018"],["dc.description.abstract","The coat protein complex I (COPI) allows the precise sorting of lipids and proteins between Golgi cisternae and retrieval from the Golgi to the ER. This essential role maintains the identity of the early secretory pathway and impinges on key cellular processes, such as protein quality control. In this Cell Science at a Glance and accompanying poster, we illustrate the different stages of COPI-coated vesicle formation and revisit decades of research in the context of recent advances in the elucidation of COPI coat structure. By calling attention to an array of questions that have remained unresolved, this review attempts to refocus the perspectives of the field."],["dc.identifier.doi","10.1242/jcs.209890"],["dc.identifier.pmid","29535154"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77706"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/25"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.haserratum","/handle/2/102924"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 3.0"],["dc.title","Formation of COPI-coated vesicles at a glance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","672"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","682"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Geva, Yosef"],["dc.contributor.author","Crissman, Jonathan"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Gómez-Navarro, Natalia"],["dc.contributor.author","Chuartzman, Silvia G."],["dc.contributor.author","Stahmer, Kyle R."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Miller, Elizabeth A."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2018-04-23T11:49:04Z"],["dc.date.available","2018-04-23T11:49:04Z"],["dc.date.issued","2017"],["dc.description.abstract","The endoplasmic reticulum (ER) is the entry site of proteins into the endomembrane system. Proteins exit the ER via coat protein II (COPII) vesicles in a selective manner, mediated either by direct interaction with the COPII coat or aided by cargo receptors. Despite the fundamental role of such receptors in protein sorting, only a few have been identified. To further define the machinery that packages secretory cargo and targets proteins from the ER to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized proteins that mediate the trafficking and maturation of Pma1, the essential yeast plasma membrane proton ATPase. Ydl121c (Exp1) is an ER protein that binds Pma1, is packaged into COPII vesicles, and whose deletion causes ER retention of Pma1. Ykl077w (Psg1) physically interacts with Exp1 and can be found in the Golgi and coat protein I (COPI) vesicles but does not directly bind Pma1. Loss of Psg1 causes enhanced degradation of Pma1 in the vacuole. Our findings suggest that Exp1 is a Pma1 cargo receptor and that Psg1 aids Pma1 maturation in the Golgi or affects its retrieval. More generally our work shows the utility of high content screens in the identification of novel trafficking components."],["dc.identifier.doi","10.1111/tra.12503"],["dc.identifier.gro","3142485"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13637"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/11"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.issn","1398-9219"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.title","Two novel effectors of trafficking and maturation of the yeast plasma membrane H+-ATPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs232124"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Huranova, Martina"],["dc.contributor.author","Estrada, Alejandro F."],["dc.contributor.author","Rau, E-Ming"],["dc.contributor.author","Spang, Anne"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2020-12-10T18:41:53Z"],["dc.date.available","2020-12-10T18:41:53Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1242/jcs.232124"],["dc.identifier.pmid","31331965"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16843"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77719"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/79"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Dissection of GTPase-activating proteins reveals functional asymmetry in the COPI coat of budding yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","370"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","379"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Weill, Uri"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Goldmann, Omer"],["dc.contributor.author","Golan, Matan"],["dc.contributor.author","Chuartzman, Silvia"],["dc.contributor.author","Munro, Sean"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2020-12-10T18:36:31Z"],["dc.date.available","2020-12-10T18:36:31Z"],["dc.date.issued","2018"],["dc.description.abstract","A third of yeast genes encode for proteins that function in the endomembrane system. However, the precise localization for many of these proteins is still uncertain. Here, we visualized a collection of ~500 N-terminally, green fluorescent protein (GFP), tagged proteins of the yeast Saccharomyces cerevisiae. By co-localizing them with 7 known markers of endomembrane compartments we determined the localization for over 200 of them. Using this approach, we create a systematic database of the various secretory compartments and identify several new residents. Focusing in, we now suggest that Lam5 resides in contact sites between the endoplasmic reticulum and the late Golgi. Additionally, analysis of interactions between the COPI coat and co-localizing proteins from our screen identifies a subset of proteins that are COPI-cargo. In summary, our approach defines the protein roster within each compartment enabling characterization of the physical and functional organization of the endomembrane system and its components."],["dc.identifier.doi","10.1111/tra.12560"],["dc.identifier.pmid","29527758"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76654"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/24"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation","SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse"],["dc.relation.issn","1398-9219"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.title","Toolbox: Creating a systematic database of secretory pathway proteins uncovers new cargo for COPI"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","831"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","842"],["dc.bibliographiccitation.volume","129"],["dc.contributor.author","Kilisch, Markus"],["dc.contributor.author","Lytovchenko, Olga"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Bertinetti, Daniela"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:54:38Z"],["dc.date.available","2017-09-07T11:54:38Z"],["dc.date.issued","2016"],["dc.description.abstract","The transport of the K+ channels TASK-1 and TASK-3 (also known as KCNK3 and KCNK9, respectively) to the cell surface is controlled by the binding of 14-3-3 proteins to a trafficking control region at the extreme C-terminus of the channels. The current model proposes that phosphorylation-dependent binding of 14-3-3 sterically masks a COPI-binding motif. However, the direct effects of phosphorylation on COPI binding and on the binding parameters of 14-3-3 isoforms are still unknown. We find that phosphorylation of the trafficking control region prevents COPI binding even in the absence of 14-3-3, and we present a quantitative analysis of the binding of all human 14-3-3 isoforms to the trafficking control regions of TASK-1 and TASK-3. Surprisingly, the affinities of 14-3-3 proteins for TASK-1 are two orders of magnitude lower than for TASK-3. Furthermore, we find that phosphorylation of a second serine residue in the C-terminus of TASK-1 inhibits 14-3-3 binding. Thus, phosphorylation of the trafficking control region can stimulate or inhibit transport of TASK-1 to the cell surface depending on the target serine residue. Our findings indicate that control of TASK-1 trafficking by COPI, kinases, phosphatases and 14-3-3 proteins is highly dynamic."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1242/jcs.180182"],["dc.identifier.gro","3141729"],["dc.identifier.isi","000370240900016"],["dc.identifier.pmid","26743085"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12874"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/424"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/100"],["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 | A07: Rolle der TRC40-Maschinerie im Proteostase-Netzwerk von Kardiomyozyten"],["dc.relation.eissn","1477-9137"],["dc.relation.issn","0021-9533"],["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","A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1"],["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.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"]]