Honemann-Capito, Mona

[["dc.bibliographiccitation.firstpage","1560"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Karuna M, Pradhipa"],["dc.contributor.author","Witte, Leonie"],["dc.contributor.author","Linnemannstoens, Karen"],["dc.contributor.author","Choezom, Dolma"],["dc.contributor.author","Danieli-Mackay, Adi"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Gross, Julia Christina"],["dc.date.accessioned","2021-04-14T08:31:10Z"],["dc.date.available","2021-04-14T08:31:10Z"],["dc.date.issued","2020"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.3390/biom10111560"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83502"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.publisher","MDPI"],["dc.relation.eissn","2218-273X"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Phosphorylation of Ykt6 SNARE Domain Regulates Its Membrane Recruitment and Activity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","dev185421"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Development"],["dc.bibliographiccitation.volume","147"],["dc.contributor.author","Linnemannstöns, Karen"],["dc.contributor.author","Witte, Leonie"],["dc.contributor.author","Karuna M, Pradhipa"],["dc.contributor.author","Kittel, Jeanette Clarissa"],["dc.contributor.author","Danieli, Adi"],["dc.contributor.author","Müller, Denise"],["dc.contributor.author","Nitsch, Lena"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Grawe, Ferdinand"],["dc.contributor.author","Wodarz, Andreas"],["dc.contributor.author","Gross, Julia Christina"],["dc.date.accessioned","2021-04-14T08:23:55Z"],["dc.date.available","2021-04-14T08:23:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/dev.185421"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81097"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1477-9129"],["dc.relation.issn","0950-1991"],["dc.title","Ykt6-dependent endosomal recycling is required for Wnt secretion in the Drosophila wing epithelium"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","71"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","80"],["dc.bibliographiccitation.volume","193"],["dc.contributor.author","Morawe, Tobias"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","von Stein, Walter"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T08:57:07Z"],["dc.date.available","2018-11-07T08:57:07Z"],["dc.date.issued","2011"],["dc.description.abstract","In Drosophila melanogaster oogenesis, there are 16 germline cells that form a cyst and stay connected to each other by ring canals. Ring canals allow the cytoplasmic transport of proteins, messenger ribonucleic acids, and yolk components from the nurse cells into the oocyte. In this paper, we describe the protein Rings lost (Rngo) and show that it is required for ring canal growth in germline cysts. rngo is an essential gene, and germline clones of a rngo-null allele show defects in ovary development, including mislocalization of ring canal proteins and fusion of germline cells. Rngo appears to be a ubiquitin receptor that possesses a ubiquitin-like domain, a ubiquitin-associated domain, and a retroviral-like aspartate protease (RVP) domain. Rngo binds to ubiquitin and to the 26S proteasome and colocalizes with both in germline cells, and its RVP domain is required for dimerization of Rngo and for its function in vivo. Our results thus show, for the first time, a function for a ubiquitin receptor in Drosophila development."],["dc.identifier.doi","10.1083/jcb.201009142"],["dc.identifier.isi","000289077100010"],["dc.identifier.pmid","21444692"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7828"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/23315"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Loss of the extraproteasomal ubiquitin receptor Rings lost impairs ring canal growth in Drosophila oogenesis"],["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","1079"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","1095"],["dc.bibliographiccitation.volume","217"],["dc.contributor.author","Beati, Hamze"],["dc.contributor.author","Peek, Irina"],["dc.contributor.author","Hordowska, Paulina"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Glashauser, Jade"],["dc.contributor.author","Renschler, Fabian A."],["dc.contributor.author","Kakanj, Parisa"],["dc.contributor.author","Ramrath, Andreas"],["dc.contributor.author","Leptin, Maria"],["dc.contributor.author","Luschnig, Stefan"],["dc.contributor.author","Wiesner, Silke"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2020-12-10T18:15:35Z"],["dc.date.available","2020-12-10T18:15:35Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1083/jcb.201610098"],["dc.identifier.eissn","1540-8140"],["dc.identifier.issn","0021-9525"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74893"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The adherens junction–associated LIM domain protein Smallish regulates epithelial morphogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","dev186833"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Development"],["dc.bibliographiccitation.volume","147"],["dc.contributor.author","Witte, Leonie"],["dc.contributor.author","Linnemannstöns, Karen"],["dc.contributor.author","Schmidt, Kevin"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Grawe, Ferdinand"],["dc.contributor.author","Wodarz, Andreas"],["dc.contributor.author","Gross, Julia Christina"],["dc.date.accessioned","2021-04-14T08:23:55Z"],["dc.date.available","2021-04-14T08:23:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1242/dev.186833"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17518"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81096"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1477-9129"],["dc.relation.issn","0950-1991"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The kinesin motor Klp98A mediates apical to basal Wg transport"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.artnumber","e1004443"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Linnemannstoens, Karen"],["dc.contributor.author","Ripp, Caroline"],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Brechtel-Curth, Katja"],["dc.contributor.author","Hedderich, Marie"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T09:38:02Z"],["dc.date.available","2018-11-07T09:38:02Z"],["dc.date.issued","2014"],["dc.description.abstract","Wnt proteins regulate many developmental processes and are required for tissue homeostasis in adult animals. The cellular responses to Wnts are manifold and are determined by the respective Wnt ligand and its specific receptor complex in the plasma membrane. Wnt receptor complexes contain a member of the Frizzled family of serpentine receptors and a co-receptor, which commonly is a single-pass transmembrane protein. Vertebrate protein tyrosine kinase 7 (PTK7) was identified as a Wnt co-receptor required for control of planar cell polarity (PCP) in frogs and mice. We found that flies homozygous for a complete knock-out of the Drosophila PTK7 homolog off track (otk) are viable and fertile and do not show PCP phenotypes. We discovered an otk paralog (otk2, CG8964), which is co-expressed with otk throughout embryonic and larval development. Otk and Otk2 bind to each other and form complexes with Frizzled, Frizzled2 and Wnt2, pointing to a function as Wnt co-receptors. Flies lacking both otk and otk2 are viable but male sterile due to defective morphogenesis of the ejaculatory duct. Overexpression of Otk causes female sterility due to malformation of the oviduct, indicating that Otk and Otk2 are specifically involved in the sexually dimorphic development of the genital tract."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pgen.1004443"],["dc.identifier.isi","000339902600007"],["dc.identifier.pmid","25010066"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10458"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32974"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7404"],["dc.relation.issn","1553-7390"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The PTK7-Related Transmembrane Proteins Off-track and Off-track 2 Are Co-receptors for Drosophila Wnt2 Required for Male Fertility"],["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","12263"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Extracellular Vesicles"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Linnemannstöns, Karen"],["dc.contributor.author","Karuna M, Pradhipa"],["dc.contributor.author","Witte, Leonie"],["dc.contributor.author","Choezom, Dolma"],["dc.contributor.author","Honemann‐Capito, Mona"],["dc.contributor.author","Lagurin, Alex Simon"],["dc.contributor.author","Schmidt, Chantal Vanessa"],["dc.contributor.author","Shrikhande, Shreya"],["dc.contributor.author","Steinmetz, Lara‐Kristin"],["dc.contributor.author","Wiebke, Möbius"],["dc.contributor.author","Gross, Julia Christina"],["dc.date.accessioned","2022-10-04T10:21:23Z"],["dc.date.available","2022-10-04T10:21:23Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1002/jev2.12263"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114397"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-600"],["dc.relation.eissn","2001-3078"],["dc.relation.issn","2001-3078"],["dc.title","Microscopic and biochemical monitoring of endosomal trafficking and extracellular vesicle secretion in an endogenous in vivo model"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1000644"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Koch, Carmen M."],["dc.contributor.author","Honemann-Capito, Mona"],["dc.contributor.author","Egger-Adam, Diane"],["dc.contributor.author","Wodarz, Andreas"],["dc.date.accessioned","2018-11-07T11:25:26Z"],["dc.date.available","2018-11-07T11:25:26Z"],["dc.date.issued","2009"],["dc.description.abstract","The epigenetic regulation of gene expression by the covalent modification of histones is a fundamental mechanism required for the proper differentiation of germ line cells during development. Trimethylation of histone 3 lysine 9 (H3K9me3) leads to chromatin silencing and the formation of heterochromatin by recruitment of heterochromatin protein 1 (HP1). dSETDB1/Eggless (Egg), the ortholog of the human methyltransferase SETDB1, is the only essential H3K9 methyltransferase in Drosophila and is required for H3K9 trimethylation in the female germ line. Here we show that Windei (Wde), the Drosophila homolog of mouse mAM and human MCAF1, is an essential cofactor of Egg required for its nuclear localization and function in female germ line cells. By deletion analysis combined with coimmunoprecipitation, we have identified the protein regions in Wde and Egg that are necessary and sufficient for the interaction between the two proteins. We furthermore identified a region of Egg that gets covalently modified by SUMOylation, which may facilitate the formation of higher order chromatin-modifying complexes. Together with Egg, Wde localizes to euchromatin, is enriched on chromosome 4, and binds to the Painting of fourth (POF) protein. Our data provide the first genetic and phenotypic analysis of a mAM/MCAF1 homolog in a model organism and demonstrate its essential function in the survival of germ line cells."],["dc.identifier.doi","10.1371/journal.pgen.1000644"],["dc.identifier.isi","270817800027"],["dc.identifier.pmid","19750210"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5809"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56619"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7390"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Windei, the Drosophila Homolog of mAM/MCAF1, Is an Essential Cofactor of the H3K9 Methyl Transferase dSETDB1/Eggless in Germ Line Development"],["dc.title.original","5809"],["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"]]