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Autor:Ye M; Zhang Y; Zhang X; Zhang J; Jing P; Cao L; Li N; Li X; Yao L; Zhang J; Zhang J
Dirección:Department of Pulmonary Medicine, Xijing Hospital, Xi'an, China.
Título:Targeting FBW7 as a Strategy to Overcome Resistance to Targeted Therapy in Non-Small Cell Lung Cancer.
Fuente:Cancer R 77(13):, 2017 Jul 01.
País de publicación:United States
Idioma:eng
Resumen:Inhibition of EGFR and anaplastic lymphoma kinase (ALK) signaling is highly effective in a subgroup of non-small cell lung cancer (NSCLC) patients with distinct clinicopathologic features. However, resistance to EGFR and ALK inhibitors inevitably occurs, and the molecular mechanism underlying resistance is not fully understood. In this study, we report a PI3K/Akt- and MEK/ERK-independent resistance mechanism by which loss of the E3 ubiquitin ligase F-box and WD repeat domain containing 7 (FBW7α) leads to targeted therapy resistance via stabilization of antiapoptotic protein MCL-1. Using a panel of
studies, we showed that the regulatory machinery responsible for MCL-1 protein degradation was a step-wise event involving phosphorylation and nucleus translocation. ERK cooperated with GSKss to phosphorylate MCL-1 Ser159 residue, which enabled MCL-1 to translocate into the nucleus and bind FBW7. Defects in this sequence impaired MCL-1 degradation and cell apoptosis, recapitulating phenotypes observed in FBW7 deficiency. Downregulation of FBW7 was found in EGFR inhibitor-resistant human NSCLC specimens and correlated with increased MCL-1 protein expression. Reactivation of FBW7 sensitized resistant cells to targeted therapy and facilitated MCL-1 degradation. Overall, our study provides proof-of-principle insight into a PI3K/Akt- and MEK/ERK-independent resistant model and suggests that targeting FBW7 can overcome resistance to targeted therapy.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Cell Cycle Proteins); 0 (F-Box Proteins); 0 (MCL1 protein, human); 0 (Myeloid Cell Leukemia Sequence 1 Protein); 0 (Protein Kinase Inhibitors); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 6.3.2.19 (FBXW7 protein, human)
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Autor:Zheng Y; Zhang X; Chen Z
Dirección:College of Pharmaceutical Sciences, Zhejiang University, Hangzhou 310058, China.
Título:[Research progress on mechanism of Nix-mediated mitophagy].
Fuente:Zhejiang Da Xue Xue Bao Yi Xue B 46(1):92-96, 2017 Jan 25.
País de publicación:China
Idioma:chi
Resumen:Autophagy is fundamental to maintain cellular homeostasis. As one kind of the most well-studied selective autophagy, autophagy of mitochondria (mitophagy)is crucial for the clearance of damaged mitochondria. Mitophagy dysfunction has been proved to be closely associated with many human diseases. Nix is a key protein for mitophagy during the maturation of reticulocytes. However, the detailed molecular mechanisms underlying Nix-mediated mitophagy are not fully understood. This article summarizes three possible working models of Nix in mitophagy induction. Firstly, Nix can interplay with Parkin, another important protein for mitophagy, to initiate mitophagy. Secondly, Nix can serve as a receptor for autophagy machinery by interacting with Atg8 family through its LIR motif. Finally, as a BH3-only protein, Nix can compete with Beclin-1 to bind other members of Bcl-2 family resulting in increased free Beclin-1 in cytosol, which further promotes autophagy flux.
Tipo de publicación:JOURNAL ARTICLE; REVIEW
Nombre de substancia:0 (Autophagy-Related Protein 8 Family); 0 (BNIP3L protein, human); 0 (Beclin-1); 0 (Membrane Proteins); 0 (Proto-Oncogene Proteins); 0 (Proto-Oncogene Proteins c-bcl-2); 0 (Tumor Suppressor Proteins); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.27 (parkin protein)
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Autor:Tawo R; Pokrzywa W; Kevei ?; Akyuz ME; Balaji V; Adrian S; H?hfeld J; Hoppe T
Dirección:Institute for Cell Biology, University of Bonn, Ulrich-Haberland Str. 61a, 53121 Bonn, Germany.
Título:The Ubiquitin Ligase CHIP Integrates Proteostasis and Aging by Regulation of Insulin Receptor Turnover.
Fuente:C 169(3):470-482.e13, 2017 Apr 20.
País de publicación:United States
Idioma:eng
Resumen:Aging is attended by a progressive decline in protein homeostasis (proteostasis), aggravating the risk for protein aggregation diseases. To understand the coordination between proteome imbalance and longevity, we addressed the mechanistic role of the quality-control ubiquitin ligase CHIP, which is a key regulator of proteostasis. We observed that CHIP deficiency leads to increased levels of the insulin receptor (INSR) and reduced lifespan of worms and flies. The membrane-bound INSR regulates the insulin and IGF1 signaling (IIS) pathway and thereby defines metabolism and aging. INSR is a direct target of CHIP, which triggers receptor monoubiquitylation and endocytic-lysosomal turnover to promote longevity. However, upon proteotoxic stress conditions and during aging, CHIP is recruited toward disposal of misfolded proteins, reducing its capacity to degrade the INSR. Our study indicates a competitive relationship between proteostasis and longevity regulation through CHIP-assisted proteolysis, providing a mechanistic concept for understanding the impact of proteome imbalance on aging.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Antigens, CD); 0 (Proteome); 0 (Somatomedins); EC 2.3.2.27 (STUB1 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.10.1 (INSR protein, human); EC 2.7.10.1 (Receptor, Insulin)
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Autor:Couch FJ; Shimelis H; Hu C; Hart SN; Polley EC; Na J; Hallberg E; Moore R; Thomas A; Lilyquist J; Feng B; McFarland R; Pesaran T; Huether R; LaDuca H; Chao EC; Goldgar DE; Dolinsky JS
Dirección:Department of Laboratory Medicine and Pathology, Mayo Clinic, Rochester, Minnesota.
Título:Associations Between Cancer Predisposition Testing Panel Genes and Breast Cancer.
Fuente:JAMA O 3(9):, 2017 Sep 01.
País de publicación:United States
Idioma:eng
Resumen:Importance: Germline pathogenic variants in BRCA1 and BRCA2 predispose to an increased lifetime risk of breast cancer. However, the relevance of germline variants in other genes from multigene hereditary cancer testing panels is not well defined. Objective: To determine the risks of breast cancer associated with germline variants in cancer predisposition genes. Design, Setting, and Participants: A study population of 65???057 patients with breast cancer receiving germline genetic testing of cancer predisposition genes with hereditary cancer multigene panels. Associations between pathogenic variants in non-BRCA1 and non-BRCA2 predisposition genes and breast cancer risk were estimated in a case-control analysis of patients with breast cancer and Exome Aggregation Consortium reference controls. The women underwent testing between March 15, 2012, and June 30, 2016. Main Outcomes and Measures: Breast cancer risk conferred by pathogenic variants in non-BRCA1 and non-BRCA2 predisposition genes. Results: The mean (SD) age at diagnosis for the 65 057 women included in the analysis was 48.5 (11.1) years. The frequency of pathogenic variants in 21 panel genes identified in 41???611 consecutively tested white women with breast cancer was estimated at 10.2%. After exclusion of BRCA1, BRCA2, and syndromic breast cancer genes (CDH1, PTEN, and TP53), observed pathogenic variants in 5 of 16 genes were associated with high or moderately increased risks of breast cancer: ATM (OR, 2.78; 95% CI, 2.22-3.62), BARD1 (OR, 2.16; 95% CI, 1.31-3.63), CHEK2 (OR, 1.48; 95% CI, 1.31-1.67), PALB2 (OR, 7.46; 95% CI, 5.12-11.19), and RAD51D (OR, 3.07; 95% CI, 1.21-7.88). Conversely, variants in the BRIP1 and RAD51C ovari the MRE11A, RAD50, and NBN MRN the MLH1 and PMS2 m and NF1 were not associated with increased risks of breast cancer. Conclusions and Relevance: This study establishes several panel genes as high- and moderate-risk breast cancer genes and provides estimates of breast cancer risk associated with pathogenic variants in these genes among individuals qualifying for clinical genetic testing.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (CDKN2A protein, human); 0 (Cell Cycle Proteins); 0 (Cyclin-Dependent Kinase Inhibitor p18); 0 (DNA-Binding Proteins); 0 (G-T mismatch-binding protein); 0 (MLH1 protein, human); 0 (MRE11A protein, human); 0 (NBN protein, human); 0 (Neurofibromin 1); 0 (Nuclear Proteins); 0 (PALB2 protein, human); 0 (RAD51C protein, human); 0 (RAD51D protein, human); 0 (Rad50 protein, human); 0 (Tumor Suppressor Proteins); EC 2.3.2.27 (BARD1 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.1.11 (Checkpoint Kinase 2); EC 2.7.11.1 (ATM protein, human); EC 2.7.11.1 (Ataxia Telangiectasia Mutated Proteins); EC 2.7.11.1 (CHEK2 protein, human); EC 3.6.1.- (BRIP1 protein, human); EC 3.6.1.- (PMS2 protein, human); EC 3.6.1.3 (MSH2 protein, human); EC 3.6.1.3 (Mismatch Repair Endonuclease PMS2); EC 3.6.1.3 (MutL Protein Homolog 1); EC 3.6.1.3 (MutS Homolog 2 Protein); EC 3.6.4.13 (RNA Helicases); EC 6.5.1.- (DNA Repair Enzymes)
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Autor:Tong J; Wang P; Tan S; Chen D; Nikolovska-Coleska Z; Zou F; Yu J; Zhang L
Dirección:University of Pittsburgh Cancer Institute, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania.
Título:Mcl-1 Degradation Is Required for Targeted Therapeutics to Eradicate Colon Cancer Cells.
Fuente:Cancer R 77(9):, 2017 May 01.
País de publicación:United States
Idioma:eng
Resumen:The Bcl-2 family protein Mcl-1 is often degraded in cancer cells subjected to effective therapeutic treatment, and defective Mcl-1 degradation has been associated with intrinsic and acquired drug resistance. However, a causal relationship between Mcl-1 degradation and anticancer drug responses has not been directly established, especially in solid tumor cells where Mcl-1 inhibition alone is insufficient to trigger cell death. In this study, we present evidence that Mcl-1 participates directly in determining effective therapeutic responses in colon cancer cells. In this setting, Mcl-1 degradation was induced by a variety of multikinase inhibitor drugs, where it relied upon GSK3ss phosphorylation and FBW7-dependent ubiquitination. Specific blockade by genetic knock-in (KI) abolished apoptotic responses and conferred resistance to kinase inhibitors.
-KI also suppressed the antiangiogenic and anti-hypoxic effects of kinase inhibitors in the tumor microenvironment. Interestingly, these same inhibitors also induced the BH3-only Bcl-2 family protein PUMA, which is required for apoptosis. Degradation-resistant Mcl-1 bound and sequestered PUMA from other prosurvival proteins to maintain cell survival, which was abolished by small-molecule Mcl-1 inhibitors. Our findings establish a pivotal role for Mcl-1 degradation in the response of colon cancer cells to targeted therapeutics, and they provide a useful rational platform to develop Mcl-1-targeting agents that can overcome drug resistance.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Cell Cycle Proteins); 0 (F-Box Proteins); 0 (MCL1 protein, human); 0 (Myeloid Cell Leukemia Sequence 1 Protein); 0 (Protein Kinase Inhibitors); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 6.3.2.19 (FBXW7 protein, human)
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Autor:Hu Y; Li W; Gao T; Cui Y; Jin Y; Li P; Ma Q; Liu X; Cao C
Dirección:State Key Laboratory of Pathogen Biosecurity, Beijing Institute of Biotechnology, Beijing, China.
Título:The Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Inhibits Type I Interferon Production by Interfering with TRIM25-Mediated RIG-I Ubiquitination.
Fuente:J V 91(8), 2017 Apr 15.
País de publicación:United States
Idioma:eng
Resumen:Severe acute respiratory syndrome (SARS) is a respiratory disease, caused by a coronavirus (SARS-CoV), that is characterized by atypical pneumonia. The nucleocapsid protein (N protein) of SARS-CoV plays an important role in inhibition of type I interferon (IFN) production via an unknown mechanism. In this study, the SARS-CoV N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation. Type I IFN production induced by poly I·C or Sendai virus (SeV) was suppressed by the SARS-CoV N protein. SARS-CoV replication was increased by overexpression of the full-length N protein but not N amino acids 1 to 361, which could not interact with TRIM25. These findings provide an insightful interpretation of the SARS-CoV-mediated host innate immune suppression caused by the N protein. The SARS-CoV N protein is essential for the viral life cycle and plays a key role in the virus-host interaction. We demonstrated that the interaction between the C terminus of the N protein and the SPRY domain of TRIM25 inhibited TRIM25-mediated RIG-I ubiquitination, which resulted in the inhibition of IFN production. We also found that the Middle East respiratory syndrome CoV (MERS-CoV) N protein interacted with TRIM25 and inhibited RIG-I signaling. The outcomes of these findings indicate the function of the coronavirus N protein in modulating the host's initial innate immune response.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Interferon Type I); 0 (Nucleocapsid Proteins); 0 (Transcription Factors); 0 (Tripartite Motif Proteins); 0 (nucleocapsid protein, Coronavirus); EC 2.3.2.27 (RNF135 protein, human); EC 2.3.2.27 (TRIM25 protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
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Autor:Saenz DT; Fiskus W; Qian Y; Manshouri T; Rajapakshe K; Raina K; Coleman KG; Crew AP; Shen A; Mill CP; Sun B; Qiu P; Kadia TM; Pemmaraju N; DiNardo C; Kim MS; Nowak AJ; Coarfa C; Crews CM; Verstovsek S; Bhalla KN
Dirección:Department of Leukemia, The University of Texas M.D. Anderson Cancer Center, Houston, TX, USA.
Título:Novel BET protein proteolysis-targeting chimera exerts superior lethal activity than bromodomain inhibitor (BETi) against post-myeloproliferative neoplasm secondary (s) AML cells.
Fuente:L 31(9):, 2017 Sep.
País de publicación:England
Idioma:eng
Resumen:The PROTAC (proteolysis-targeting chimera) ARV-825 recruits bromodomain and extraterminal (BET) proteins to the E3 ubiquitin ligase cereblon, leading to degradation of BET proteins, including BRD4. Although the BET-protein inhibitor (BETi) OTX015 caused accumulation of BRD4, treatment with equimolar concentrations of ARV-825 caused sustained and profound depletion (>90%) of BRD4 and induced significantly more apoptosis in cultured and patient-derived (PD) CD34+ post-MPN sAML cells, while relatively sparing the CD34+ normal hematopoietic progenitor cells. RNA-Seq, Reverse Phase Protein Array and mass cytometry 'CyTOF' analyses demonstrated that ARV-825 caused greater perturbations in messenger RNA (mRNA) and protein expressions than OTX015 in sAML cells. Specifically, compared with OTX015, ARV-825 treatment caused more robust and sustained depletion of c-Myc, CDK4/6, JAK2, p-STAT3/5, PIM1 and Bcl-xL, while increasing the levels of p21 and p27. Compared with OTX015, PROTAC ARV-771 treatment caused greater reduction in leukemia burden and further improved survival of NSG mice engrafted with luciferase-expressing HEL92.1.7 cells. Co-treatment with ARV-825 and JAK inhibitor ruxolitinib was synergistically lethal against established and PD CD34+ sAML cells. Notably, ARV-825 induced high levels of apoptosis in the in vitro generated ruxolitinib-persister or ruxolitinib-resistant sAML cells. These findings strongly support the in vivo testing of the BRD4-PROTAC based combinations against post-MPN sAML.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (ARV-825); 0 (Antigens, CD34); 0 (Azepines); 0 (BRD4 protein, human); 0 (INCB018424); 0 (Nuclear Proteins); 0 (Pyrazoles); 0 (Transcription Factors); 4Z8R6ORS6L (Thalidomide); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
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Autor:Shoji S; Hanada K; Ohsawa N; Shirouzu M
Dirección:Division of Structural and Synthetic Biology, RIKEN Center for Life Science Technologies, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan shisako.shoji@riken.jp mikako.shirouzu@riken.jp.
Título:Central catalytic domain of BRAP (RNF52) recognizes the types of ubiquitin chains and utilizes oligo-ubiquitin for ubiquitylation.
Fuente:Biochem J; 474(18):, 2017 Sep 07.
País de publicación:England
Idioma:eng
Resumen:Really interesting new gene (RING)-finger protein 52 (RNF52), an E3 ubiquitin ligase, is found in eukaryotes from yeast to humans. Human RNF52 is known as breast cancer type 1 susceptibility protein (BRCA1)-associated protein 2 (BRAP or BRAP2). The central catalytic domain of BRAP comprises four subdomains: nucleotide-binding α/ss plait (NBP), really interesting new gene (RING) zinc finger, ubiquitin-specific protease (UBP)-like zinc finger (ZfUBP), and coiled-coil (CC). This domain architecture is conserved in RNF52 however, the domain's function in the ubiquitin system has not been delineated. In the present study, we discovered that the RNF52 domain, comprising NBP-RING-ZfUBP-CC, binds to ubiquitin chains (oligo-ubiquitin) but not to the ubiquitin monomers, and can utilize various ubiquitin chains for ubiquitylation and auto-ubiquitylation. The RNF52 domain preferentially bound to M1- and K63-linked di-ubiquitin chains, weakly to K27-linked chains, but not to K6-, K11-, or K48-linked chains. The binding preferences of the RNF52 domain for ubiquitin-linkage types corresponded to ubiquitin usage in the ubiquitylation reaction, except for K11-, K29-, and K33-linked chains. Additionally, the RNF52 domain directly ligated the intact M1-linked, tri-, and tetra-ubiquitin chains and recognized the structural alterations caused by the phosphomimetic mutation of these ubiquitin chains. Full-length BRAP had nearly the same specificity for the ubiquitin-chain types as the RNF52 domain alone. Mass spectrometry analysis of oligomeric ubiquitylation products, mediated by the RNF52 domain, revealed that the ubiquitin-linkage types and auto-ubiquitylation sites depend on the length of ubiquitin chains. Here, we propose a model for the oligomeric ubiquitylation process, controlled by the RNF52 domain, which is not a sequential assembly process involving monomers.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Ubiquitin); EC 2.3.2.23 (UBE2D1 protein, human); EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes); EC 2.3.2.27 (BRAP protein, human); EC 2.3.2.27 (Ubiquitin-Protein Ligases)
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Autor:Kampmeyer C; Karakostova A; Schenstr?m SM; Abildgaard AB; Lauridsen AM; Jourdain I; Hartmann-Petersen R
Dirección:From the Linderstr?m-Lang Center, Department of Biology, University of Copenhagen, Ole Maal?es Vej 5, 2200 Copenhagen N, Denmark and.
Título:The exocyst subunit Sec3 is regulated by a protein quality control pathway.
Fuente:J Biol C 292(37):, 2017 Sep 15.
País de publicación:United States
Idioma:eng
Resumen:Exocytosis involves fusion of secretory vesicles with the plasma membrane, thereby delivering membrane proteins to the cell surface and releasing material into the extracellular space. The tethering of the secretory vesicles before membrane fusion is mediated by the exocyst, an essential phylogenetically conserved octameric protein complex. Exocyst biogenesis is regulated by several processes, but the mechanisms by which the exocyst is degraded are unknown. Here, to unravel the components of the exocyst degradation pathway, we screened for extragenic suppressors of a temperature-sensitive fission yeast strain mutated in the exocyst subunit Sec3 ( ). One of the suppressing DNAs encoded a truncated dominant-negative variant of the 26S proteasome subunit, Rpt2, indicating that exocyst degradation is controlled by the ubiquitin-proteasome system. The temperature-dependent growth defect of the
strain was gene dosage-dependent and suppressed by blocking the proteasome, Hsp70-type molecular chaperones, the Pib1 E3 ubiquitin-protein ligase, and the deubiquitylating enzyme Ubp3. Moreover, defects in cell septation, exocytosis, and endocytosis in
mutant strains were similarly alleviated by mutation of components in this pathway. We also found that, particularly under stress conditions, wild-type Sec3 degradation is regulated by Pib1 and the 26S proteasome. In conclusion, our results suggest that a cytosolic protein quality control pathway monitors folding and proteasome-dependent turnover of an exocyst subunit and, thereby, controls exocytosis in fission yeast.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Enzyme Inhibitors); 0 (HSP70 Heat-Shock Proteins); 0 (Recombinant Fusion Proteins); 0 (Schizosaccharomyces pombe Proteins); 0 (Sec3 protein, S pombe); 0 (Vesicular Transport Proteins); 0 (sks2 protein, S pombe); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.4.- (Endopeptidases); EC 3.4.19.12 (Deubiquitinating Enzymes); EC 3.4.25.1 (Proteasome Endopeptidase Complex); EC 3.4.99.- (rpt2 protein, S pombe)
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Autor:Flack JE; Mieszczanek J; Novcic N; Bienz M
Dirección:MRC Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge, CB2 0QH, UK.
Título:Wnt-Dependent Inactivation of the Groucho/TLE Co-repressor by the HECT E3 Ubiquitin Ligase Hyd/UBR5.
Fuente:Mol C 67(2):181-193.e5, 2017 Jul 20.
País de publicación:United States
Idioma:eng
Resumen:Extracellular signals are transduced to the cell nucleus by effectors that bind to enhancer complexes to operate transcriptional switches. For example, the Wnt enhanceosome is a multiprotein complex associated with Wnt-responsive enhancers through T cell factors (TCF) and kept silent by Groucho/TLE co-repressors. Wnt-activated ss-catenin binds to TCF to overcome this repression, but how it achieves this is unknown. Here, we discover that this process depends on the HECT E3 ubiquitin ligase Hyd/UBR5, which is required for Wnt signal responses in Drosophila and human cell lines downstream of activated Armadillo/ss-catenin. We identify Groucho/TLE as a functionally relevant substrate, whose ubiquitylation by UBR5 is induced by Wnt signaling and conferred by ss-catenin. Inactivation of TLE by UBR5-dependent ubiquitylation also involves VCP/p97, an AAA ATPase regulating the folding of various cellular substrates including ubiquitylated chromatin proteins. Thus, Groucho/TLE ubiquitylation by Hyd/UBR5 is a key prerequisite that enables Armadillo/ss-catenin to activate transcription.
Tipo de publicación:JOURNAL ARTICLE
Nombre de substancia:0 (Armadillo Domain Proteins); 0 (Basic Helix-Loop-Helix Transcription Factors); 0 (CTNNB1 protein, human); 0 (Cell Cycle Proteins); 0 (Co-Repressor Proteins); 0 (Drosophila Proteins); 0 (Repressor Proteins); 0 (TLE3 protein, human); 0 (Transcription Factors); 0 (armadillo protein, Drosophila); 0 (beta Catenin); 0 (groucho protein, Drosophila); EC 2.3.2.26 (UBR5 protein, human); EC 2.3.2.26 (hyperplastic discs protein, Drosophila); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 3.6.1.- (Adenosine Triphosphatases); EC 3.6.1.- (CDC48 protein); EC 3.6.1.- (VCP protein, Drosophila)
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PalabrasDescriptor de asuntoDescriptor de asunto primarioLímitesAutorPalabras del títuloPalabras del resumenIdiomaPaís de publicaciónNombre de substanciaNombre personal como asuntoRevistaAsunto de RevistaISSNTipo de publicaciónIdentificador únicoMes de ingresoA?o de publicaciónTexto completoActualización por claseCategoria DeCSCategoria DeCS explodidaCategoria CIE-10SubSetsPaís de AfiliaciónAfiliaciónAfiliación 2
PalabrasDescriptor de asuntoDescriptor de asunto primarioLímitesAutorPalabras del títuloPalabras del resumenIdiomaPaís de publicaciónNombre de substanciaNombre personal como asuntoRevistaAsunto de RevistaISSNTipo de publicaciónIdentificador únicoMes de ingresoA?o de publicaciónTexto completoActualización por claseCategoria DeCSCategoria DeCS explodidaCategoria CIE-10SubSetsPaís de AfiliaciónAfiliaciónAfiliación 2
PalabrasDescriptor de asuntoDescriptor de asunto primarioLímitesAutorPalabras del títuloPalabras del resumenIdiomaPaís de publicaciónNombre de substanciaNombre personal como asuntoRevistaAsunto de RevistaISSNTipo de publicaciónIdentificador únicoMes de ingresoA?o de publicaciónTexto completoActualización por claseCategoria DeCSCategoria DeCS explodidaCategoria CIE-10SubSetsPaís de AfiliaciónAfiliaciónAfiliación 2
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