Function of the SNARE Ykt6 on autophagosomes requires the Dsl1 complex and the Atg1 kinase complex

DC FieldValueLanguage
dc.contributor.authorGao, Jieqiong
dc.contributor.authorKurre, Rainer
dc.contributor.authorRose, Jaqueline
dc.contributor.authorWalter, Stefan
dc.contributor.authorFroehlich, Florian
dc.contributor.authorPiehler, Jacob
dc.contributor.authorReggiori, Fulvio
dc.contributor.authorUngermann, Christian
dc.date.accessioned2021-12-23T16:10:46Z-
dc.date.available2021-12-23T16:10:46Z-
dc.date.issued2020
dc.identifier.issn1469221X
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/9385-
dc.description.abstractThe mechanism and regulation of fusion between autophagosomes and lysosomes/vacuoles are still only partially understood in both yeast and mammals. In yeast, this fusion step requires SNARE proteins, the homotypic vacuole fusion and protein sorting (HOPS) tethering complex, the RAB7 GTPase Ypt7, and its guanine nucleotide exchange factor (GEF) Mon1-Ccz1. We and others recently identified Ykt6 as the autophagosomal SNARE protein. However, it has not been resolved when and how lipid-anchored Ykt6 is recruited onto autophagosomes. Here, we show that Ykt6 is recruited at an early stage of the formation of these carriers through a mechanism that depends on endoplasmic reticulum (ER)-resident Dsl1 complex and COPII-coated vesicles. Importantly, Ykt6 activity on autophagosomes is regulated by the Atg1 kinase complex, which inhibits Ykt6 through direct phosphorylation. Thus, our findings indicate that the Ykt6 pool on autophagosomal membranes is kept inactive by Atg1 phosphorylation, and once an autophagosome is ready to fuse with vacuole, Ykt6 dephosphorylation allows its engagement in the fusion event.
dc.description.sponsorshipALW Open Program [ALWOP.310]; ZonMW TOP [91217002]; Open Competition ENW-KLEIN [OCENW.KLEIN.118]; Marie Sklodowska-Curie Cofund [713660]; Marie Sklodowska-Curie ITN [765912]; Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [UN111/7-3, UN111/13-1]; iBiOs funds of the DFG; Projekt DEAL; [Sonderforschungsbereich 944]; We thank Angela Perz and Kathrin Auffarth for expert technical assistance. F. Reggiori was supported by ALW Open Program (ALWOP.310), ZonMW TOP (91217002), an Open Competition ENW-KLEIN (OCENW.KLEIN.118), Marie Sklodowska-Curie Cofund (713660), and Marie Sklodowska-Curie ITN (765912) grants. C. Ungermann was supported by a grant of the Deutsche Forschungsgemeinschaft (UN111/7-3 and 13-1) and the Sonderforschungsbereich 944 (Project P11). R. Kurre and J. Piehler were supported by the Sonderforschungsbereich 944 (Projekt Z01) and the iBiOs funds of the DFG. Open access funding enabled and organized by Projekt DEAL.
dc.language.isoen
dc.publisherWILEY
dc.relation.ispartofEMBO REPORTS
dc.subjectautophagy
dc.subjectBiochemistry & Molecular Biology
dc.subjectCell Biology
dc.subjectCOPII vesicles
dc.subjectDsl1 complex
dc.subjectEARLY STEPS
dc.subjectEARLY-STAGE
dc.subjectENDOPLASMIC RETICULUM RETRIEVAL
dc.subjectGOLGI
dc.subjectPROTEIN
dc.subjectR-SNARE
dc.subjectSACCHAROMYCES-CEREVISIAE
dc.subjectSNARE
dc.subjectTETHERING COMPLEX
dc.subjectVESICLE FORMATION
dc.subjectYEAST
dc.subjectYkt6
dc.titleFunction of the SNARE Ykt6 on autophagosomes requires the Dsl1 complex and the Atg1 kinase complex
dc.typejournal article
dc.identifier.doi10.15252/embr.202050733
dc.identifier.isiISI:000598572300015
dc.description.volume21
dc.description.issue12
dc.contributor.orcid0000-0003-2652-2686
dc.contributor.orcid0000-0001-8307-2189
dc.identifier.eissn14693178
dc.publisher.place111 RIVER ST, HOBOKEN 07030-5774, NJ USA
dcterms.isPartOf.abbreviationEMBO Rep.
dcterms.oaStatushybrid, Green Published
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptSonderforschungsbereich 944: Physiologie und Dynamik zellulärer Mikrokompartimente-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.deptidorganisation19-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-6872-6567-
crisitem.author.orcid0000-0001-8307-2189-
crisitem.author.orcid0000-0002-2143-2270-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgFB 05 - Biologie/Chemie-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.grandparentorgUniversität Osnabrück-
crisitem.author.netidKuRa617-
crisitem.author.netidFrFl166-
crisitem.author.netidPiJa938-
crisitem.author.netidUnCh999-
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