Wodarz, Andreas

[["dc.bibliographiccitation.firstpage","636"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Current Biology"],["dc.bibliographiccitation.lastpage","642"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Klopfenstein, Dieter Robert"],["dc.contributor.author","Fischer, Nannette"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T08:44:08Z"],["dc.date.available","2018-11-07T08:44:08Z"],["dc.date.issued","2010"],["dc.description.abstract","Cell polarity in higher animals is controlled by evolutionarily conserved protein complexes, which localize to the cytocortex in a polarized manner [1, 2]. The PAR-3/PAR-6/atypical protein kinase C (aPKC) complex is the first to become asymmetrically localized, and it controls the localization of additional complexes functioning further downstream in the regulation of cell polarity [3-9]. The first component of the PAR-3/PAR-6/aPKC complex that is localized to the cortex is Bazooka/PAR-3 (Baz), a large scaffolding protein [10]. In most cell types analyzed, loss of Baz function leads to loss of cell polarity [6, 8, 11]. Here we present a structure-function analysis of Baz focusing on its subcellular localization and function in four different polarized Drosophila cell types: the embryonic ectodermal epidermis, the follicular epithelium, embryonic neuroblasts, and the oocyte. We show that the PDZ domains of Baz are dispensable for its correct localization, whereas a conserved region in the C-terminal part of Baz to which no function had been assigned so far is required and sufficient for membrane localization. This region binds to phosphoinositide membrane lipids and thus mediates cortical localization of Baz by direct interaction with the plasma membrane. Our findings reveal a mechanism for the coupling of plasma membrane polarity and cortical polarity."],["dc.identifier.doi","10.1016/j.cub.2010.01.065"],["dc.identifier.isi","000276753100028"],["dc.identifier.pmid","20303268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/20129"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","0960-9822"],["dc.title","Membrane Targeting of Bazooka/PAR-3 Is Mediated by Direct Binding to Phosphoinositide Lipids"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T11:17:29Z"],["dc.date.available","2018-11-07T11:17:29Z"],["dc.date.issued","2008"],["dc.format.extent","14"],["dc.identifier.isi","000255316100025"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54816"],["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","Dephosphorylation of Bazooka by PP2A is required for proper apical-basal polarity in embryonic neuroblasts"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","153"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","154"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T11:25:40Z"],["dc.date.available","2018-11-07T11:25:40Z"],["dc.date.issued","2009"],["dc.description.abstract","Activation of Notch by its transmembrane ligand Delta requires the E3 ubiquitin ligases Neuralized or Mind bomb and endocytosis of the ubiquitinated ligand. In this issue of Developmental Cell, Ossipova et al. show that the polarity regulator PAR-1 phosphorylates Mind bomb, leading to the degradation of Mind bomb and to changes in cell fate due to loss of Notch signaling."],["dc.identifier.doi","10.1016/j.devcel.2009.07.018"],["dc.identifier.isi","000269138600002"],["dc.identifier.pmid","19686673"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56675"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1534-5807"],["dc.title","Notch Signaling: Linking Delta Endocytosis and Cell Polarity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","15"],["dc.bibliographiccitation.lastpage","27"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T09:14:46Z"],["dc.date.available","2018-11-07T09:14:46Z"],["dc.date.issued","2012"],["dc.description.abstract","Many cell types in animals and plants are polarized, which means that the cell is subdivided into functionally and structurally distinct compartments. Epithelial cells, for example, possess an apical side facing a lumen or the outside environment and a basolateral side facing adjacent epithelial cells and the basement membrane. Neurons possess distinct axonal and dendritic compartments with specific functions in sending and receiving signals. Migrating cells form a leading edge that actively engages in pathfinding and cell-substrate attachment, and a trailing edge where such attachments are abandoned. In all of these cases, both the plasma membrane and the cytocortex directly underneath the plasma membrane show differences in their molecular composition and structural organization. In this chapter we will focus on a specific type of membrane lipids, the phosphoinositides, because in polarized cells they show a polarized distribution in the plasma membrane. They furthermore influence the molecular organization of the cytocortex by recruiting specific protein binding partners which are involved in the regulation of the cytoskeleton and in signal transduction cascades that control polarity, growth and cell migration."],["dc.identifier.doi","10.1042/BSE0530015"],["dc.identifier.isi","000310713700002"],["dc.identifier.pmid","22928505"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27498"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Portland Press Ltd"],["dc.publisher.place","London"],["dc.relation.isbn","978-1-85578-189-4"],["dc.relation.ispartof","CELL POLARITY AND CANCER"],["dc.relation.issn","0071-1365"],["dc.title","Phosphoinositide lipids and cell polarity: linking the plasma membrane to the cytocortex"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","751"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","760"],["dc.bibliographiccitation.volume","190"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Bueckers, Johanna"],["dc.contributor.author","Kastrup, Lars"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T08:39:17Z"],["dc.date.available","2018-11-07T08:39:17Z"],["dc.date.issued","2010"],["dc.description.abstract","A pical-basal polarity in Drosophila melanogaster epithelia depends on several evolutionarily conserved proteins that have been assigned to two distinct protein complexes: the Bazooka (Baz)-PAR-6 (partitioning defective 6)-atypical protein kinase C (aPKC) complex and the Crumbs (Crb)-Stardust (Sdt) complex. These proteins operate in a functional hierarchy, in which Baz is required for the proper subcellular localization of all other proteins. We investigated how these proteins interact and how this interaction is regulated. We show that Baz recruits Sdt to the plasma membrane by direct interaction between the Postsynaptic density 95/Discs large/Zonula occludens 1 (PDZ) domain of Sdt and a region of Baz that contains a phosphorylation site for aPKC. Phosphorylation of Baz causes the dissociation of the Baz-Sdt complex. Overexpression of a nonphosphorylatable version of Baz blocks the dissociation of Sdt from Baz, causing phenotypes very similar to those of crb and sdt mutations. Our findings provide a molecular mechanism for the phosphorylation-dependent interaction between the Baz-PAR-3 and Crb complexes during the establishment of epithelial polarity."],["dc.identifier.doi","10.1083/jcb.201006029"],["dc.identifier.isi","000281781300007"],["dc.identifier.pmid","20819933"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/6295"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18957"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Formation of a Bazooka-Stardust complex is essential for plasma membrane polarity in epithelia"],["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","528"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biology Open"],["dc.bibliographiccitation.lastpage","U137"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Shahab, Jaffer"],["dc.contributor.author","Tiwari, Manu D."],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T09:58:28Z"],["dc.date.available","2018-11-07T09:58:28Z"],["dc.date.issued","2015"],["dc.description.abstract","Apico-basal polarity is the defining characteristic of epithelial cells. In Drosophila, apical membrane identity is established and regulated through interactions between the highly conserved Par complex (Bazooka/Par3, atypical protein kinase C and Par6), and the Crumbs complex (Crumbs, Stardust and PATJ). It has been proposed that Bazooka operates at the top of a genetic hierarchy in the establishment and maintenance of apico-basal polarity. However, there is still ambiguity over the correct sequence of events and cross-talk with other pathways during this process. In this study, we reassess this issue by comparing the phenotypes of the commonly used baz(4) and baz(815-8) alleles with those of the so far uncharacterized baz(XR11) and baz(EH747) null alleles in different Drosophila epithelia. While all these baz alleles display identical phenotypes during embryonic epithelial development, we observe strong discrepancies in the severity and penetrance of polarity defects in the follicular epithelium: polarity is mostly normal in baz(EH747) and baz(XR11) while baz(4) and baz(815-8) show loss of polarity, severe multilayering and loss of epithelial integrity throughout the clones. Further analysis reveals that the chromosomes carrying the baz(4) and baz(815-8) alleles may contain additional mutations that enhance the true baz loss-of-function phenotype in the follicular epithelium. This study clearly shows that Baz is dispensable for the regulation of polarity in the follicular epithelium, and that the requirement for key regulators of cell polarity is highly dependent on developmental context and cell type."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1242/bio.201410934"],["dc.identifier.isi","000353175400011"],["dc.identifier.pmid","25770183"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11847"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37369"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","2046-6390"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","Bazooka/PAR3 is dispensable for polarity in Drosophila follicular epithelial cells"],["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","901"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","908"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Krahn, Michael P."],["dc.contributor.author","Egger-Adam, Diane"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T08:28:42Z"],["dc.date.available","2018-11-07T08:28:42Z"],["dc.date.issued","2009"],["dc.description.abstract","Bazooka/Par-3 (Baz) is a key regulator of cell polarity in epithelial cells and neuroblasts (NBs). Phosphorylation of Baz by PAR-1 and aPKC is required for its function in epithelia, but little is known about the dephosphorylation mechanisms that antagonize the activities of these kinases or about the relevance of Baz phosphorylation for NB polarity. We found that protein phosphatase 2A (PP2A) binds to Baz via its structural A subunit. By using phospho-specific antibodies, we show that PP2A dephosphorylates; Baz at the conserved serine residue 1085 and thereby antagonizes the kinase activity of PAR-1. Loss of PP2A function leads to complete reversal of polarity in NBs, giving rise to an \"upside-down\" polarity phenotype. Overexpression of PAR-1 or Baz, or mutation of 14-3-3 proteins that bind phosphorylated Baz, causes essentially the same phenotype, indicating that the balance of PAR-1 and PP2A effects on Baz phosphorylation determines NIB polarity."],["dc.description.sponsorship","Deutsche Forschungsgemenschaft [SFB 590, TP A2, WO 584/4-1, 4-2]"],["dc.identifier.doi","10.1016/j.devcel.2009.04.011"],["dc.identifier.isi","000267203700016"],["dc.identifier.pmid","19531360"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16484"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1534-5807"],["dc.title","PP2A Antagonizes Phosphorylation of Bazooka by PAR-1 to Control Apical-Basal Polarity in Dividing Embryonic Neuroblasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]