Arakel, Eric Clement

[["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"]]