Auswahl der wissenschaftlichen Literatur zum Thema „UBTD1“
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Zeitschriftenartikel zum Thema "UBTD1"
Zhang, Xiao-Wei, Xiao-Feng Wang, Su-Jie Ni, Wei Qin, Li-Qin Zhao, Rui-Xi Hua, You-Wei Lu, Jin Li, Goberdhan P. Dimri und Wei-Jian Guo. „UBTD1 induces cellular senescence through an UBTD1-Mdm2/p53 positive feedback loop“. Journal of Pathology 235, Nr. 4 (07.01.2015): 656–67. http://dx.doi.org/10.1002/path.4478.
Der volle Inhalt der QuelleUhler, Jay P., Henrik Spåhr, Géraldine Farge, Stéphan Clavel, Nils-Göran Larsson, Maria Falkenberg, Tore Samuelsson und Claes M. Gustafsson. „The UbL protein UBTD1 stably interacts with the UBE2D family of E2 ubiquitin conjugating enzymes“. Biochemical and Biophysical Research Communications 443, Nr. 1 (Januar 2014): 7–12. http://dx.doi.org/10.1016/j.bbrc.2013.10.137.
Der volle Inhalt der QuelleYang, Nan, Tianxiang Chen, Liang Wang, Runkun Liu, Yongshen Niu, Liankang Sun, Bowen Yao et al. „CXCR4 mediates matrix stiffness-induced downregulation of UBTD1 driving hepatocellular carcinoma progression via YAP signaling pathway“. Theranostics 10, Nr. 13 (2020): 5790–801. http://dx.doi.org/10.7150/thno.44789.
Der volle Inhalt der QuelleBlueggel, Mike, Johannes van den Boom, Hemmo Meyer, Peter Bayer und Christine Beuck. „Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase“. Biomolecules 9, Nr. 12 (14.12.2019): 876. http://dx.doi.org/10.3390/biom9120876.
Der volle Inhalt der QuelleTremblay, Michel G., Dany S. Sibai, Melissa Valère, Jean-Clément Mars, Frédéric Lessard, Roderick T. Hori, Mohammad Moshahid Khan, Victor Y. Stefanovsky, Mark S. LeDoux und Tom Moss. „Ribosomal DNA promoter recognition is determined in vivo by cooperation between UBTF1 and SL1 and is compromised in the UBTF-E210K neuroregression syndrome“. PLOS Genetics 18, Nr. 2 (09.02.2022): e1009644. http://dx.doi.org/10.1371/journal.pgen.1009644.
Der volle Inhalt der QuelleZhen, M., R. Heinlein, D. Jones, S. Jentsch und E. P. Candido. „The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating enzyme involved in selective protein degradation“. Molecular and Cellular Biology 13, Nr. 3 (März 1993): 1371–77. http://dx.doi.org/10.1128/mcb.13.3.1371-1377.1993.
Der volle Inhalt der QuelleZhen, M., R. Heinlein, D. Jones, S. Jentsch und E. P. Candido. „The ubc-2 gene of Caenorhabditis elegans encodes a ubiquitin-conjugating enzyme involved in selective protein degradation.“ Molecular and Cellular Biology 13, Nr. 3 (März 1993): 1371–77. http://dx.doi.org/10.1128/mcb.13.3.1371.
Der volle Inhalt der QuelleProphet, Sarah M., Brigitte S. Naughton und Christian Schlieker. „p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells“. International Journal of Molecular Sciences 23, Nr. 9 (21.04.2022): 4627. http://dx.doi.org/10.3390/ijms23094627.
Der volle Inhalt der QuelleKern, Maximilian, Vanesa Fernandez-Sáiz, Zasie Schäfer und Alexander Buchberger. „UBXD1 binds p97 through two independent binding sites“. Biochemical and Biophysical Research Communications 380, Nr. 2 (März 2009): 303–7. http://dx.doi.org/10.1016/j.bbrc.2009.01.076.
Der volle Inhalt der QuelleRamkumar, Poornima, Bennett A. Smith, Anu C. Akinbamidele, Joseph Kapcia, Stephen L. Beauparlant und Dale S. Haines. „Generation and Characterization of Novel Monoclonal Antibodies Recognizing UBXD1“. Hybridoma 28, Nr. 6 (Dezember 2009): 459–62. http://dx.doi.org/10.1089/hyb.2009.0035.
Der volle Inhalt der QuelleDissertationen zum Thema "UBTD1"
Tiroille, Victor. „Ingénierie génétique d'organoïdes à l'aide de nanoblades et étude du rôle d'UBTD1 comme modulateur de la force d'adhésion cellulaire dans les organoïdes de prostate“. Electronic Thesis or Diss., Université Côte d'Azur, 2021. http://theses.univ-cotedazur.fr/2021COAZ6039.
Der volle Inhalt der QuelleDuring my thesis, I worked on the 3D organoid model following two main objectives: i) developing genetic tools to modify the genome of organoids and ii) deciphering the role of ubiquitin domain-containing protein 1 (UBTD1) in the development of prostate organoids . Genome engineering has become in the last few years more accessible thanks to the RNA programmable endonucleases such as the CRISPR-Cas9 system. However, using this editing technology in synthetic organs called ‘organoids’ is still very inefficient. This is mainly due to the delivery methods used for the CRISPR-Cas9 machinery, which are predominantly performed by electroporation of RNPs containing the CAS9-gRNA complex, a procedure toxic for the organoids. Here we describe the use of the ‘Nanoblade’ technology to accomplish genome editing in organoids. Nanoblades outperformed by far knockout (KO) levels achieved with other techniques used to date for delivery of the gene editing machinery. We reached up to 80% of gene knockout in organoids after treatment with nanoblades. We achieved high-level nanoblade-mediated KO for the androgen receptor (AR) encoding gene and the cystic fibrosis transmembrane conductance regulator (CFTR) gene with single gRNA or dual gRNA containing nanoblades. Most importantly, in contrast to other gene editing methods, this was obtained without toxicity for the organoids. Moreover, it requires only four weeks to obtain stable lines KO for a gene in organoids and no obvious unwanted INDELS in off-target site in the genome were detected. In conclusion, nanoblades simplify and allow rapid genome editing in organoids with little to no side-effects.Morphogenesis and tissue remodeling are finely regulated processes governed by cell-cell adhesions. However, the spatial and temporal control of adhesion molecules remains partially unexplored. Here we studied the role of UBTD1 as a modulator of the strength of adherens in the prostate epithelium. We showed that down-regulation of UBTD1 disrupted the self- organization of cells in three dimensions. Conversely, we demonstrated that overexpression of UBTD1 induced more regular epithelial monolayers and increased cell surface tension. Transcriptomic analyses revealed a gene expression profile of proteins involved in cell junctions affected by UBTD1 modulation. Using the prostate organoid model, we showed that UBTD1 expression in luminal cells disrupted cyst formation in mouse prostate organoids. Finally using a co-immunoprecipitation approach coupled to mass spectrometry, we showed that UBTD1 interacts with partners involved in cell-cell junctions and that these interactants have their expression modulated by UBTD1 deregulation. Our results show that a protein involved in protein degradation processes regulates the strength of adherens junctions
Kyle, Dane Brittan. „Characterization of a UBXD1 Polymorphic Variant and Identification of UBXD1 Interacting Proteins“. Master's thesis, Temple University Libraries, 2011. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/148616.
Der volle Inhalt der QuelleM.S.
p97, a member of the AAA ATPase (ATPases Associated with diverse cellular Activities) family of proteins, exists as a hexamer with two centrally located ATPase domains D1 and D2. The ATPase function of p97 is the means by which mechanical force is applied to substrates, consequently changing their conformation. As a highly abundant protein within cells, p97 has been shown to function in multiple pathways whereby specificity is directed via adaptor proteins. The largest family of bona fide p97 adaptors is the `Ubiquitin regulatory X' (UBX) domain containing family of adaptors. In addition to the UBX domain containing family of adaptors, proteins containing a PUB domain have been implicated in binding to p97. The p97 adaptor protein UBXD1 contains both a UBX and PUB domain, however the UBX domain does not participate in binding p97 due to absence of the conserved motif required for binding. Recently, a highly conserved region within the first 150 amino acids of the UBXD1 N-terminus has been shown to participate in p97 binding (Kern et al., 2009). The cellular function of UBXD1 remains largely unknown. One of the focuses of the Haines laboratory is to elucidate the function of UBXD1. Unpublished results from within the laboratory suggest UBXD1 to be defective at interacting with p97 mutants found in Inclusion Body Myopathy associated with Paget's Disease of Bone and Frontotemporal Dementia (IBMPFD) and Amyotrophic Lateral Sclerosis (ALS) disease, leading to a disruption of the autophagy pathway. These results suggest a role for UBXD1 as a human disease relevant protein. Search of a Single Nucleotide Polymorphism (SNP) database for polymorphisms within conserved regions of UBXD1 was carried out. Interestingly, the SNP database revealed a polymorphic variant within a conserved region of the PUB domain. The SNP was found within the asparagine residue of the evolutionarily conserved surface patch, resulting in an asparagine(N) to serine(S) substitution, termed N184S. The two main objectives of my master's thesis project are 1) to characterize this UBXD1 polymorphic variant in terms of p97 binding capabilities and determine the prevalence of the N184S PUB domain SNP within the population and 2) identification/verification of UBXD1 interacting proteins that may provide a clue for UBXD1 function in autophagy and define domains required for association. As a result of interaction-based studies, I have been able to show a severe loss-of-binding phenotype by the UBXD1 N184S polymorphic variant. While the N184S PUB domain SNP could not be validated within my sample population, the interaction data led to the discovery of potential UBXD1 interacting proteins. Additionally, proteomics data generated by Dr. Dale Haines in the lab of Dr. Raymond Deshaies revealed ERGIC-53 to be a novel binding partner of UBXD1. Through interaction-based studies, I have been able to determine the regions required for the interaction between UBXD1 and ERGIC-53 as well as propose a possible role for p97 UBXD1 complexes in autophagy.
Temple University--Theses
Beauparlant, Stephen Lewis. „Functional characterization of the p97 adaptor protein UBXD1“. Diss., Temple University Libraries, 2011. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/213118.
Der volle Inhalt der QuellePh.D.
p97 is a member of the AAA family of proteins (ATPase Associated with various cellular Activities). It is a highly conserved and abundant protein and functions in numerous ubiquitin-mediated processes including ERAD. Endoplasmic Reticulum Associated Degradation is the process by which misfolded/ubiquitinated proteins translocate out of the ER and migrate to the proteasome for degradation. p97 maintains substrate misfolding and mediates its exit from the ER and trafficking to the 26S proteasome. It also plays important roles in protein trafficking, the cell-cycle, apoptosis and homeotypic Golgi Apparatus and Endoplasmic Reticulum membrane fusion after mitosis. In addition, p97 plays a role in the aggresome-autophagy degradation pathway, which handles the ubiquitin-mediated destruction of aggregate-prone, misfolded, cytosolic proteins. p97 mutation is the causative alteration in the disorder, IBMPFD, which is marked by defects in autophagy. This broad diversity of function is mediated through p97's interaction with a large group of adaptor proteins. Many of these adaptors harbor both p97 interaction motifs and ubiquitin association domains. However, more than half of known p97 adaptors do not. Their function is largely unknown. UBXD1 is one known adaptor for p97 that does not have a ubiquitin association domain (UBA), and has been shown to have decreased interaction with IBMPFD mutant p97R155H and p97A232E. Recently, it has been suggested to perform a role in protein trafficking, specifically in monoubiquitinated caveolin-1 internalization and trafficking to the endosome. A novel high abundance UBXD1 interacting partner has been identified via solution-based mass spectrometric analyses. ERGIC-53, the namesake of the ER-Golgi Intermediate Compartment, has been shown to be involved in bi-directional trafficking between the ER and Golgi. The association between UBXD1 and ERGIC-53 is unique among UBX family members. Deletional analysis has shown that unlike p97, the ERGIC-53-UBXD1 interaction takes place in the extreme amino terminus of UBXD1, (within the first 10 amino acids) which is predicted by computer modeling to form a hydrophobic binding pocket. Further site-directed mutagenesis work has clearly shown four amino acids (3 highly hydrophobic) are crucial for maintaining this interaction. They have been modeled to form a conserved alpha-helix. ßCOPI, a primary member of the COPI coatomer complex which is involved in protectively coating ERGIC-53 positive vesicles, is also thought to be involved with the ERGIC-53-UBXD1-p97 pathway. ßCOPI has been identified as a UBXD1-independent interactor with p97. Modest UBXD1 over- expression using a ponasterone inducible system has shown that UBXD1 modulates ERGIC-53 localization. Additionally, a functional link between UBXD1, p97 and ERGIC-53 in autophagy has been discovered through the use of a highly efficient, miR30-based, inducible knockdown system. Upon individual knockdown of UBXD1, p97 and ERGIC-53, autophagic markers p62 and LC3-II accumulate at relatively high levels in normal culture conditions, strongly suggesting a role in mediating basal autophagy. However, when placed under starvation conditions, autophagy progresses and p62 is degraded. It is speculated from these studies that a p97/UBXD1 complex plays a role in regulating the trafficking of ERGIC-53 positive vesicles and this activity plays an important role in autophagy.
Temple University--Theses
Wollny, Claudia [Verfasser], und Alexander [Gutachter] Buchberger. „Der p97-Kofaktor UBXD1 ist ein neuer Regulator des NF-kB-Signalweges / Claudia Wollny ; Gutachter: Alexander Buchberger“. Würzburg : Universität Würzburg, 2019. http://d-nb.info/1182902634/34.
Der volle Inhalt der QuelleTrusch, Franziska [Verfasser], Peter [Akademischer Betreuer] Bayer und Hemmo [Akademischer Betreuer] Meyer. „Strukturelle Charakterisierung des N-Terminus von UBXD1 und seine Regulation der ATPase-Aktivität von p97 / Franziska Trusch. Gutachter: Hemmo Meyer. Betreuer: Peter Bayer“. Duisburg, 2014. http://d-nb.info/1062492633/34.
Der volle Inhalt der QuelleKirchner, Philipp [Verfasser], Hemmo [Akademischer Betreuer] Meyer und Michael [Akademischer Betreuer] Ehrmann. „The role of ubiquitination and the p97-UBXD1 complex in regulating endosomal trafficking of caveolin-1 / Philipp Kirchner. Gutachter: Michael Ehrmann. Betreuer: Hemmo Meyer“. Duisburg, 2015. http://d-nb.info/1074102355/34.
Der volle Inhalt der QuelleBOSSO, GIUSEPPE. „Effete/UbcD1, a Drosophila ubiquitin conjugating enzyme, involved in genome stability“. Doctoral thesis, 2016. http://hdl.handle.net/11573/874587.
Der volle Inhalt der QuelleDuring my three PhD years, I focused my interest on the study of Eff/UbcD1, a well conserved protein known to be involved in telomere protection in Drosophila. Mutations in the effete/UbcD1 gene, that encodes a highly evolutionarily conserved ubiquitin-conjugating enzyme, lead to frequent Telomeric Fusions (TFs) in Drosophila mitotic cells, indicating that Effete/UbcD1 is required for telomere protection. However, little is known about the molecular mechanism underlying this function. Recent work has shown that Effete/UbcD1 is a chromatin component that on polytene chromosomes strongly co-localizes with Heterochromatin Protein 1 (HP1), a well-known chromatin factor that is also required to prevent TFs. In the first part of my thesis, I describe results on the genetic and molecular relationship between UbcD1 and HP1. Intriguingly, I describe that loss of Eff/UbcD1 in a Hp1 mutant background yields to a frequency of TFs lower than that observed in the single Hp1 mutants, suggesting that protective functions at telomeres of both Eff/UbcD1 and HP1 are strongly interconnected. My biochemical analyses reveal that Eff/UbcD1 physically interacts with and ubiquitinates HP1 and that HP1 itself is able to bind ubiquitin in a non covalent manner. Furthermore, I also demonstrate that Eff/UbcD1 promotes the enrichment of a novel and slow migrating isoform of HP1 (sHP1) that was not described before. Moreover, I describe a previously uncharacterized functional relationship involving HP1, the MRN complex and histone H3. By site-specific mutagenesis, I identified at least 2 different lysines required for HP1 ubiquitination. Of these, Lys151 arises as a key residue for ubiquitination of sHP1 and more importantly, I demonstrate that Lys151 ubiquitination is required for regulating the stability of both MRN complex and histone H3. In the second part of my thesis, I also show results that indicate a role for Eff/UbcD1 in DNA repair. I describe that loss of Eff/UbcD1, but not the Drosophila Rad6 ortholog UbcD6, confers radioresistance after X-ray irradiation. My cytological analysis of mitotic chromosomes reveals that in Eff/UbcD1 mitotic cells the frequencies of chromosome breaks (CBs), chromosome aberrations (CABs) and irradiation induced foci (IRIF) are all significantly reduced after X-ray compared to control. However, the number of X-ray induced CBS and CABs increases when Eff/UbcD1 is overexpressed indicating that Eff/UbcD1 plays a negative role in the DNA damage response (DDR) and/or repair. Moreover, my western blot analysis also indicate that the MRN complex is required for Eff/UbcD1 stability. In addition, Co-IP experiments reveal that Eff/UbcD1 interacts with the MRN complex member Rad50. However, Rad50 protein levels are not affected in eff/UbcD1 mutants, indicating that if Eff/UbcD1 is involved in Rad50 ubiquitination, this modification is not required for Rad50 degradation. Taken together, my results suggest that Eff/UbcD1 plays important roles in the regulation of chromosome stability by interacting with both telomeric and DDR factors.
Wollny, Claudia. „Der p97-Kofaktor UBXD1 ist ein neuer Regulator des NF-kB-Signalweges“. Doctoral thesis, 2019. https://nbn-resolving.org/urn:nbn:de:bvb:20-opus-132430.
Der volle Inhalt der QuelleThe essential, ubiquitin-selective ATPase p97 regulates a variety of cellular processes in eukaryotes. Among others, these include protein quality control, DNA repair, signal-transduction, cell cycle control, autophagy and the endolysosomal system. The distinct functions of p97 are tightly controlled by regulatory cofactors. UBX domain-containing proteins are the largest and best studied group of p97 cofactors . They are characterized by a UBX domain, which mediates binding to p97. The family-member UBXD1 is highly conserved in higher eukaryotes and possesses at least two additional p97 binding modules, a PUB domain and a VIM motif. While UBXD1 can localize to vesicles of the endolysosomal degradation system, its exact cellular function is still poorly understood. The aim of this study was the functional characterisation of human UBXD1. To that end, candidates of a previous yeast two-hybrid screen were tested for their two-hybrid interaction with different UBXD1 variants. Immunoprecipitation experiments were used to analyse if the candidates also interact with UBXD1 in mammalian cells. This led to the identification of the ubiquitin-ligase TRIAD3A and the ubiquitin-editing protein A20 as promising new binding partners of UBXD1. Moreover, it could be demonstrated that the interaction between UBXD1 and A20 depends on a functional PUB domain and the seventh zinc finger motif of A20. Because both TRIAD3A and A20 are negative regulators of the NF-B signaling pathway, it was subsequently tested if UBXD1 also has a function in NF-B signaling. Indeed, UBXD1-depleted HeLa 57A cells showed a strongly reduced NF B dependent expression of a reporter gene after activation of the signaling pathway by TNF, IL-1, Doxorubicin and H2O2. The reduced activity observed after various stimuli argues for a general role of UBXD1 in the NF-B signaling pathway. Quantitative real-time PCR demonstrated that the expression of endogenous NF-B target genes in HeLa and HEK293T cells was also reduced upon UBXD1-depletion. Since the nuclear translocation of the NF-B subunit p65 upon stimulation with TNF or IL-1was also reduced in UBXD1-depleted cells, UBXD1 is likely to participate in an earlier phase of NF-B activation. It is possible that UBXD1 regulates a known function of A20 and influences for example the binding of A20 to endocytic vesicles or to linear ubiquitin chains. In summary, this work describes a novel function of the p97 cofactor UBXD1 as a positive regulator of the NF-B signaling pathway