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AuthorLeidner, Juliadc.contributor.author
Date of accession2016-03-15T06:23:23Zdc.date.accessioned
Available in OPARU since2016-03-15T06:23:23Zdc.date.available
Year of creation2010dc.date.created
AbstractThe NF-kappaB-transcription factor RelB plays an important role during the development of lymphatic tissues, for the inflammatory response and during tumorigenesis. RelB acts as a key component of the alternative NF-kappaB signalling pathway. However, RelB also modulates the classical NF-kappaB signalling pathway by acting as transcriptional activator and repressor. Until now, the molecular mechanisms underlying this functional diversity are largely unknown. Yet, the previously described proteasomal RelB-degradation in activated T cells represents one mechanism for the regulation of RelB. Therefore, one aim of this dissertation was to prove the involvement of the degradation-inducing Lys48-linked ubiquitinylation within the process of RelB-degradation. Indeed, the inducible RelB-degradation was accompanied by an increasing polyubiquitinylation. Furthermore, a basal non-proteasomal ubiquitinylation of RelB was observed that could be linked to an increase of the transcriptional activity of RelB. The molecular mechanism underlying this positive ubiquitin-effect could not be solved completely, yet the obtained results point to alterations in cofactor-interactions by the ubiquitinylated RelB. The SUMOylation is another lysine-specific posttranslational modification that is able to affect cofactor-interactions and to antagonize the ubiquitinylation. Indeed, RelB-modifications by SUMO were observed. Functionally, the SUMOylation seems to antagonize RelB-ubiquitinylation as it appears to have a negative effect on RelB activity. In summary, the presented results display a new mechanism for regulating the transcriptional activity of RelB by ubiquitinylation and SUMOylation, which is unique among the NF-kappaB family.dc.description.abstract
Languagededc.language.iso
PublisherUniversität Ulmdc.publisher
LicenseStandard (Fassung vom 01.10.2008)dc.rights
Link to license texthttps://oparu.uni-ulm.de/xmlui/license_v2dc.rights.uri
KeywordRelBdc.subject
KeywordSUMOdc.subject
Dewey Decimal GroupDDC 570 / Life sciencesdc.subject.ddc
MeSHTranscription factor RelBdc.subject.mesh
TitleDie Rolle Lysin-spezifischer posttranslationaler Modifikationen für die Funktion des NF-kappaB-Faktors RelBdc.title
Resource typeDissertationdc.type
DOIhttp://dx.doi.org/10.18725/OPARU-1833dc.identifier.doi
PPN621070327dc.identifier.ppn
URNhttp://nbn-resolving.de/urn:nbn:de:bsz:289-vts-72299dc.identifier.urn
GNDNuklearfaktor Kappa Bdc.subject.gnd
GNDUbiquitindc.subject.gnd
GNDUbiquitin-ähnliche Proteinedc.subject.gnd
FacultyFakultät für Naturwissenschaftenuulm.affiliationGeneral
Date of activation2010-03-04T15:12:50Zuulm.freischaltungVTS
Peer reviewneinuulm.peerReview
Shelfmark print versionZ: J-H 13.590; W: W-H 12.021uulm.shelfmark
DCMI TypeTextuulm.typeDCMI
VTS-ID7229uulm.vtsID
CategoryPublikationenuulm.category
University Bibliographyjauulm.unibibliographie


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