Gailite, Ieva

[["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Gailite, I."],["dc.contributor.author","Egger-Adam, Diane"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T11:17:30Z"],["dc.date.available","2018-11-07T11:17:30Z"],["dc.date.issued","2008"],["dc.format.extent","51"],["dc.identifier.isi","000255316100130"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54821"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.publisher.place","Jena"],["dc.relation.conference","31st Annual Meeting of the German-Society-for-Cell-Biology"],["dc.relation.eventlocation","Marburg, GERMANY"],["dc.relation.issn","0171-9335"],["dc.title","Analysis of CG14782, a new interaction partner of Bazooka, in Drosophila development"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","433"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","447"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Gailite, Ieva"],["dc.contributor.author","Egger-Adam, Diane"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T09:13:50Z"],["dc.date.available","2018-11-07T09:13:50Z"],["dc.date.issued","2012"],["dc.description.abstract","Endocytosis regulates multiple cellular processes, including the protein composition of the plasma membrane, intercellular signaling, and cell polarity. We have identified the highly conserved protein Rush hour (Rush) and show that it participates in the regulation of endocytosis. Rush localizes to endosomes via direct binding of its FYVE (Fab1p, YOTB, Vac1p, EEA1) domain to phosphatidylinositol 3-phosphate. Rush also directly binds to Rab GDP dissociation inhibitor (Gdi), which is involved in the activation of Rab proteins. Homozygous rush mutant flies are viable but show genetic interactions with mutations in Gdi, Rab5, hrs, and carnation, the fly homologue of Vps33. Overexpression of Rush disrupts progression of endocytosed cargo and increases late endosome size. Lysosomal marker staining is decreased in Rush-overexpressing cells, pointing to a defect in the transition between late endosomes and lysosomes. Rush also causes formation of endosome clusters, possibly by affecting fusion of endosomes via an interaction with the class C Vps/homotypic fusion and vacuole protein-sorting (HOPS) complex. These results indicate that Rush controls trafficking from early to late endosomes and from late endosomes to lysosomes by modulating the activity of Rab proteins."],["dc.identifier.doi","10.1091/mbc.E11-02-0154"],["dc.identifier.isi","000300409900004"],["dc.identifier.pmid","22160599"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27258"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.relation.issn","1059-1524"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","The phosphoinositide-associated protein Rush hour regulates endosomal trafficking in Drosophila"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3759"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","3771"],["dc.bibliographiccitation.volume","122"],["dc.contributor.author","Kim, Soya"],["dc.contributor.author","Gailite, Ieva"],["dc.contributor.author","Moussian, Bernard"],["dc.contributor.author","Luschnig, Stefan"],["dc.contributor.author","Goette, Maik"],["dc.contributor.author","Fricke, Karen"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Grubmüller, Helmut"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2017-09-07T11:46:47Z"],["dc.date.available","2017-09-07T11:46:47Z"],["dc.date.issued","2009"],["dc.description.abstract","Polarity of many cell types is controlled by a protein complex consisting of Bazooka/PAR-3 (Baz), PAR-6 and atypical protein kinase C (aPKC). In Drosophila, the Baz-PAR-6-aPKC complex is required for the control of cell polarity in the follicular epithelium, in ectodermal epithelia and neuroblasts. aPKC is the main signaling component of this complex that functions by phosphorylating downstream targets, while the PDZ domain proteins Baz and PAR-6 control the subcellular localization and kinase activity of aPKC. We compared the mutant phenotypes of an aPKC null allele with those of four novel aPKC alleles harboring point mutations that abolish the kinase activity or the binding of aPKC to PAR-6. We show that these point alleles retain full functionality in the control of follicle cell polarity, but produce strong loss-of-function phenotypes in embryonic epithelia and neuroblasts. Our data, combined with molecular dynamics simulations, show that the kinase activity of aPKC and its ability to bind PAR-6 are only required for a subset of its functions during development, revealing tissue-specific differences in the way that aPKC controls cell polarity."],["dc.identifier.doi","10.1242/jcs.052514"],["dc.identifier.gro","3143041"],["dc.identifier.isi","000270570800019"],["dc.identifier.pmid","19789180"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/511"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9533"],["dc.title","Kinase-activity-independent functions of atypical protein kinase C in Drosophila"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]