Stegmüller, Judith

[["dc.bibliographiccitation.artnumber","e57530"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Vadhvani, Mayur"],["dc.contributor.author","Schwedhelm-Domeyer, Nicola"],["dc.contributor.author","Mukherjee, Chaitali"],["dc.contributor.author","Stegmüller, Judith"],["dc.date.accessioned","2019-07-09T11:54:16Z"],["dc.date.available","2019-07-09T11:54:16Z"],["dc.date.issued","2013-02-28"],["dc.description.abstract","Neuronal development requires proper migration, polarization and establishment of axons and dendrites. Growing evidence identifies the ubiquitin proteasome system (UPS) with its numerous components as an important regulator of various aspects of neuronal development. F-box proteins are interchangeable subunits of the Cullin-1 based E3 ubiquitin ligase, but only a few family members have been studied. Here, we report that the centrosomal E3 ligase FBXO31-SCF (Skp1/ Cullin-1/F-box protein) regulates neuronal morphogenesis and axonal identity. In addition, we identified the polarity protein Par6c as a novel interaction partner and substrate targeted for proteasomal degradation in the control of axon but not dendrite growth. Finally, we ascribe a role for FBXO31 in dendrite growth and neuronal migration in the developing cerebellar cortex. Taken together, we uncovered the centrosomal E3 ligase FBXO31-SCF as a novel regulator of neuronal development."],["dc.format.extent","13"],["dc.identifier.doi","10.1371/journal.pone.0057530"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8725"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/60609"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The Centrosomal E3 Ubiquitin Ligase FBXO31-SCF Regulates Neuronal Morphogenesis and Migration"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","626"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Cell Death and Differentiation"],["dc.bibliographiccitation.lastpage","642"],["dc.bibliographiccitation.volume","22"],["dc.contributor.author","Matz, A."],["dc.contributor.author","Lee, S. J."],["dc.contributor.author","Schwedhelm-Domeyer, Nicola"],["dc.contributor.author","Zanini, Damiano"],["dc.contributor.author","Holubowska, Anna"],["dc.contributor.author","Kannan, M."],["dc.contributor.author","Farnworth, M. S."],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Göpfert, Martin C."],["dc.contributor.author","Stegmueller, Judith"],["dc.date.accessioned","2018-11-07T09:59:20Z"],["dc.date.available","2018-11-07T09:59:20Z"],["dc.date.issued","2015"],["dc.description.abstract","Neuronal health is essential for the long-term integrity of the brain. In this study, we characterized the novel E3 ubiquitin ligase ring finger protein 157 (RNF157), which displays a brain-dominant expression in mouse. RNF157 is a homolog of the E3 ligase mahogunin ring finger-1, which has been previously implicated in spongiform neurodegeneration. We identified RNF157 as a regulator of survival in cultured neurons and established that the ligase activity of RNF157 is crucial for this process. We also uncovered that independently of its ligase activity, RNF157 regulates dendrite growth and maintenance. We further identified the adaptor protein APBB1 (amyloid beta precursor protein-binding, family B, member 1 or Fe65) as an interactor and proteolytic substrate of RNF157 in the control of neuronal survival. Here, the nuclear localization of Fe65 together with its interaction partner RNA-binding protein SART3 (squamous cell carcinoma antigen recognized by T cells 3 or Tip110) is crucial to trigger apoptosis. In summary, we described that the E3 ligase RNF157 regulates important aspects of neuronal development."],["dc.identifier.doi","10.1038/cdd.2014.163"],["dc.identifier.isi","000350857200012"],["dc.identifier.pmid","25342469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37565"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-5403"],["dc.relation.issn","1350-9047"],["dc.title","Regulation of neuronal survival and morphology by the E3 ubiquitin ligase RNF157"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2008"],["dc.bibliographiccitation.issue","18"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2025"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Vingill, Siv"],["dc.contributor.author","Brockelt, David"],["dc.contributor.author","Lancelin, Camille"],["dc.contributor.author","Tatenhorst, Lars"],["dc.contributor.author","Dontcheva, Guergana"],["dc.contributor.author","Preisinger, Christian"],["dc.contributor.author","Schwedhelm-Domeyer, Nicola"],["dc.contributor.author","Joseph, Sabitha"],["dc.contributor.author","Mitkovski, Miso"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Schulz, Joerg B."],["dc.contributor.author","Marquardt, Till"],["dc.contributor.author","Lingor, Paul"],["dc.contributor.author","Stegmueller, Judith"],["dc.date.accessioned","2018-11-07T10:08:31Z"],["dc.date.available","2018-11-07T10:08:31Z"],["dc.date.issued","2016"],["dc.description.abstract","Mutations in the FBXO7 (PARK15) gene have been implicated in a juvenile form of parkinsonism termed parkinsonian pyramidal syndrome (PPS), characterized by Parkinsonian symptoms and pyramidal tract signs. FBXO7 (F-box protein only 7) is a subunit of the SCF (SKP1/cullin-1/F-box protein) E3 ubiquitin ligase complex, but its relevance and function in neurons remain to be elucidated. Here, we report that the E3 ligase FBXO7-SCF binds to and ubiquitinates the proteasomal subunit PSMA2. In addition, we show that FBXO7 is a proteasome-associated protein involved in proteasome assembly. In FBXO7 knockout mice, we find reduced proteasome activity and early-onset motor deficits together with premature death. In addition, we demonstrate that NEX (neuronal helix-loop-helix protein-1)-Cre-induced deletion of the FBXO7 gene in forebrain neurons or the loss of FBXO7 in tyrosine hydroxylase (TH)-positive neurons results in motor defects, reminiscent of the phenotype in PARK15 patients. Taken together, our study establishes a vital role for FBXO7 in neurons, which is required for proper motor control and accentuates the importance of FBXO7 in proteasome function."],["dc.identifier.doi","10.15252/embj.201593585"],["dc.identifier.isi","000384084900006"],["dc.identifier.pmid","27497298"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39477"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","Loss of FBXO7 (PARK15) results in reduced proteasome activity and models a parkinsonism-like phenotype in mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]