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Academic literature on the topic 'Cullin-1'

Author: Grafiati
Published: 10 December 2022
Last updated: 29 January 2023

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Journal articles on the topic "Cullin-1"

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Zhou, Yun-Hai, Jiazeng Xia, Wen-Huan Xu, Xiqi Zhu, Xiao-Hong Wu, Dong Hua, and Chungen Xing. "Cullin-1 Promotes Cell Proliferation in Human Breast Cancer and is Related to Diabetes." International Journal of Biological Markers 31, no. 4 (October 2016): 375–81. http://dx.doi.org/10.5301/jbm.5000215.

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Aim Breast carcinoma (BCA) and diabetes mellitus (DM) are two major health problems in women and the general population. Cullin-1 is reported to be an important tumor-related protein involved in cell-cycle progression, signal transduction and transcription. The aim of this work is to investigate the role of Cullin-1 in the development of BCA and to find potential relationships between Cullin-1 and diabetes in BCA patients. Methods To evaluate the function of Cullin-1, we entered 168 patients with primary invasive BCA in this study. Pairs of BCA tissues and adjacent noncancerous tissues from these patients were collected between 2006 and 2008. We used immunohistochemistry to analyze the correlation between Cullin-1 expression and clinicopathological variables and patient survival. In addition, we investigated the role of Cullin-1 in BCA cell proliferation. Results Cullin-1 expression was upregulated in BCA tissues. Enhanced immunoreactivity for Cullin-1 in BCA tissues was inversely correlated with overall survival and disease-free survival, which suggested a poor prognosis in BCA patients. Strong expression of Cullin-1 was more frequently observed in patients with estrogen receptor negativity and HER2 positivity. We also found that Cullin-1 expression was increased in BCA patients with a previous diagnosis of diabetes. Conclusions Our results demonstrate that increased Cullin-1 expression is significantly correlated with poor prognosis in patients with BCA. Cullin-1 might regulate BCA cell proliferation through the ubiquitin-proteasome system. Thus, Cullin-1 might be an important marker and a therapeutic target in BCA.
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Huang, Guochang, Andrew J. Kaufman, Y. Ramanathan, and Bhuvanesh Singh. "SCCRO (DCUN1D1) Promotes Nuclear Translocation and Assembly of the Neddylation E3 Complex." Journal of Biological Chemistry 286, no. 12 (January 19, 2011): 10297–304. http://dx.doi.org/10.1074/jbc.m110.203729.

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SCCRO/DCUN1D1/DCN1 (squamous cell carcinoma-related oncogene/defective in cullin neddylation 1 domain containing 1/defective in cullin neddylation) serves as an accessory E3 in neddylation by binding to cullin and Ubc12 to allow efficient transfer of Nedd8. In this work we show that SCCRO has broader, pleiotropic effects that are essential for cullin neddylation in vivo. Reduced primary nuclear localization of Cul1 accompanying decreased neddylation and proliferation in SCCRO−/− mouse embryonic fibroblasts led us to investigate whether compartmentalization plays a regulatory role. Decreased nuclear localization, neddylation, and defective proliferation in SCCRO−/− mouse embryonic fibroblasts were rescued by transgenic expression of SCCRO. Expression of reciprocal SCCRO and Cul1-binding mutants confirmed the requirement for SCCRO in nuclear translocation and neddylation of cullins in vivo. Nuclear translocation of Cul1 by tagging with a nuclear localization sequence allowed neddylation independent of SCCRO, but at a lower level. We found that in the nucleus, SCCRO enhances recruitment of Ubc12 to Cul1 to promote neddylation. These findings suggest that SCCRO has an essential role in neddylation in vivo involving nuclear localization of neddylation components and recruitment and proper positioning of Ubc12.
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Chadha, Attinder, France Moreau, Shanshan Wang, Antoine Dufour, and Kris Chadee. "Entamoeba histolytica activation of caspase-1 degrades cullin that attenuates NF-κB dependent signaling from macrophages." PLOS Pathogens 17, no. 9 (September 9, 2021): e1009936. http://dx.doi.org/10.1371/journal.ppat.1009936.

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While Entamoeba histolytica (Eh)-induced pro-inflammatory responses are critical in disease pathogenesis, the downstream signaling pathways that subsequently dampens inflammation and the immune response remains unclear. Eh in contact with macrophages suppresses NF-κB signaling while favoring NLRP3-dependent pro-inflammatory cytokine production by an unknown mechanism. Cullin-1 and cullin-5 (cullin-1/5) assembled into a multi-subunit RING E3 ubiquitin ligase complex are substrates for neddylation that regulates the ubiquitination pathway important in NF-κB activity and pro-inflammatory cytokine production. In this study, we showed that upon live Eh contact with human macrophages, cullin-1/4A/4B/5 but not cullin-2/3, were degraded within 10 minutes. Similar degradation of cullin-1/5 were observed from colonic epithelial cells and proximal colonic loops tissues of mice inoculated with live Eh. Degradation of cullin-1/5 was dependent on Eh-induced activation of caspase-1 via the NLRP3 inflammasome. Unlike cullin-4B, the degradation of cullin-4A was partially dependent on caspase-1 and was inhibited with a pan caspase inhibitor. Cullin-1/5 degradation was dependent on Eh cysteine proteinases EhCP-A1 and EhCP-A4, but not EhCP-A5, based on pharmacological inhibition of the cysteine proteinases and EhCP-A5 deficient parasites. siRNA silencing of cullin-1/5 decreased the phosphorylation of pIκ-Bα in response to Eh and LPS stimulation and downregulated NF-κB-dependent TNF-α mRNA expression and TNF-α and MCP-1 pro-inflammatory cytokine production. These results unravel a unique outside-in strategy employed by Eh to attenuate NF-κB-dependent pro-inflammatory responses via NLRP3 activation of caspase-1 that degraded cullin-1/5 from macrophages.
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Murali, Sathish K., Robert Little, Søren B. Poulsen, Mohammed Z. Ferdaus, David H. Ellison, James A. McCormick, and Robert A. Fenton. "Potassium Effects on NCC Are Attenuated during Inhibition of Cullin E3–Ubiquitin Ligases." Cells 11, no. 1 (December 29, 2021): 95. http://dx.doi.org/10.3390/cells11010095.

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The thiazide-sensitive sodium chloride cotransporter (NCC) plays a vital role in maintaining sodium (Na+) and potassium (K+) homeostasis. NCC activity is modulated by with-no-lysine kinases 1 and 4 (WNK1 and WNK4), the abundance of which is controlled by the RING-type E3 ligase Cullin 3 (Cul3) and its substrate adapter Kelch-like protein 3. Dietary K+ intake has an inverse correlation with NCC activity, but the mechanism underlying this phenomenon remains to be fully elucidated. Here, we investigated the involvement of other members of the cullin family in mediating K+ effects on NCC phosphorylation (active form) and abundance. In kidneys from mice fed diets varying in K+ content, there were negative correlations between NCC (phosphorylated and total) and active (neddylated) forms of cullins (Cul1, 3, 4, and 5). High dietary K+ effects on phosphorylated NCC were attenuated in Cul3 mutant mice (CUL3-Het/Δ9). Short-term (30 min) and long-term (24 h) alterations in the extracellular K+ concentration did not affect cullin neddylation levels in ex vivo renal tubules. In the short term, the ability of high extracellular K+ to decrease NCC phosphorylation was preserved in the presence of MLN4924 (pan-cullin inhibitor), but the response to low extracellular K+ was absent. In the long term, MLN4924 attenuated the effects of high extracellular K+ on NCC phosphorylation, and responses to low extracellular K+ were absent. Our data suggest that in addition to Cul3, other cullins are involved in mediating the effects of K+ on NCC phosphorylation and abundance.
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Hammill, Jared T., Daniel C. Scott, Jaeki Min, Michele C. Connelly, Gloria Holbrook, Fangyi Zhu, Amy Matheny, et al. "Piperidinyl Ureas Chemically Control Defective in Cullin Neddylation 1 (DCN1)-Mediated Cullin Neddylation." Journal of Medicinal Chemistry 61, no. 7 (March 16, 2018): 2680–93. http://dx.doi.org/10.1021/acs.jmedchem.7b01277.

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Makbruri, Makbruri, Isabella Kurnia Liem, Ahmad Aulia Jusuf, and Tantri Hellyanti. "The Dynamics of Cullin-1 Expression in Preeclamptic Placenta and its Association with Pregnancy Termination Time." Open Access Macedonian Journal of Medical Sciences 8, B (May 22, 2020): 210–15. http://dx.doi.org/10.3889/oamjms.2020.3665.

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BACKGROUND: Preeclampsia is a systemic syndrome occurring in 3–5% of pregnancies, caused by disorders of cellular factors resulting in the disruption of trophoblast differentiation and invasion which is important for the placental development and maintaining pregnancy. Cullin-1 is a protein that plays a role in the process of maintaining pregnancy, development, and trophoblast invasion in the placenta. Until now, there have been no studies linking the expression of cullin-1 in preeclamptic patients with the timing of pregnancy termination. AIM: This study analyzed cullin-1 expression in preeclamptic patients and their relationship to the timing of pregnancy termination was carried out. METHODS: Placental samples were taken from preeclampsia patients consisting of three gestational age groups, then immunohistochemical staining was performed to see the dynamics of expression and distribution in each age group of pregnancy and to find out their relationship with the timing of pregnancy termination. RESULTS: Cullin-1 was expressed in syncytiotrophoblasts and cytotrophoblasts. The lowest cullin-1 level was obtained in the very preterm age group, and the highest was found in the moderate preterm gestational age group. There was a significant difference between cullin-1 optical density (OD) expression and termination time of pregnancy, and there was a significant difference (OD) in cullin-1 preeclamptic patients with very preterm gestational age with moderate preterm gestational age. CONCLUSION: Cullin-1 was expressed both in syncytiotrophoblasts and cytotrophoblasts and was associated with the timing of pregnancy termination.
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Driscoll, James, Elias J. Anaissie, and Sajjeev Jagannathan. "Cullin-1 Controls The Clinical and Cellular response to Bortezomib Through NF-Kb Pathway Activation In Myeloma." Blood 122, no. 21 (November 15, 2013): 4445. http://dx.doi.org/10.1182/blood.v122.21.4445.4445.

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The Ubiquitin (Ub)+Proteasome system (UPS) is a highly complex network that maintains cellular homeostasis through the selective turnover of targeted proteins. The proteasome serves as the catalytic core of the UPS to execute the efficient removal of ubiquitin-conjugated proteins. Pharmacologic inhibitors that exploit the pivotal role of the proteasome in cellular metabolism promote tumor cytotoxicity and yield durable clinical responses that have significantly improved survival of patients diagnosed with the invariably fatal plasma cell malignancy multiple myeloma (MM). However, while functional blockade of the proteasome has emerged as a successful anti-cancer strategy, drug resistance inevitably emerges through mechanisms that remain elusive. Since E3 Ub ligases target biologically-relevant proteins for proteasomal degradation and are frequently overexpressed in cancers, we hypothesized that altered E3 Ub ligase expression served as a mechanism of resistance to proteasome inhibitors (PIs). To address the role of individual E3s in myelomagenegesis, gene expression profiles of MM patient samples obtained prior to treatment were analyzed. Results indicated that Cullin-1 was overexpressed in MM patient tumor samples compared to normal or MGUS samples. Cullin-1 is an essential scaffolding component of multiple Skp1-Cullin-1-F-box protein E3 complexes that mediate the ubiquitination of proteins involved in cell cycle progression. Next. bone marrow-derived CD138+ plasma cells were obtained from MM patients that were then treated with the PI bortezomib. Samples were similarly probed to identify differences in E3 expression and to identify features that dictate therapeutic response. Again, Cullin-1 was overexpressed in samples from MM patients that did not respond to bortezomib but Cullin-1 was not overexpressed in samples from those patients that responded to bortezomib. Cullin-1 levels were also higher in bortezomib-resistant myeloma cell lines and drug-resistant cells were re-sensitized to bortezomib after short-hairpin-RNA-mediated Cul-1 knockdown. Cells overexpressing Cullin-1 displayed increased NF-Kappa B activity and a reduced sensitivity to bortezomib-induced apoptosis as demonstrated by staining for annexin-positivity. The effect of Cullin-1 expression level on the sensitivity to bortezomib treatment was determined using MM xenografts in athymic SCID mice. We have used a biologically-supervised, microarray-based approach to identify Cul-1 overexpression in a subset of myeloma patients and correlated expression with clinical resistance to bortezomib. Functional studies demonstrated that Cullin-1 sustains activation of the NF-Kappa B pathway and decreases cellular response to bortezomib in vitro in human cell lines. We conclude that Cullin-1 attenuates bortezomib anti-MM activity by maintaining NF-Kappa B signaling and hence promoting tumor survival. Engineered overexpression or shRNA-mediated inactivation of Cullin-1 modulated the cytotoxic effect of bortezomib to further recapitulate the premise that tumor genomics dictate therapeutic response. Cullin-1 is a novel effector within the UPS that offers promise as an oncologic target either alone or in synergistic combination with proteasome inhibitors. Disclosures: No relevant conflicts of interest to declare.
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Lange, Stephan, Sue Perera, Phildrich Teh, and Ju Chen. "Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover." Molecular Biology of the Cell 23, no. 13 (July 2012): 2490–504. http://dx.doi.org/10.1091/mbc.e12-01-0052.

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Protein turnover through cullin-3 is tightly regulated by posttranslational modifications, the COP9 signalosome, and BTB/POZ-domain proteins that link cullin-3 to specific substrates for ubiquitylation. In this paper, we report how potassium channel tetramerization domain containing 6 (KCTD6) represents a novel substrate adaptor for cullin-3, effectively regulating protein levels of the muscle small ankyrin-1 isoform 5 (sAnk1.5).Binding of sAnk1.5 to KCTD6, and its subsequent turnover is regulated through posttranslational modification by nedd8, ubiquitin, and acetylation of C-terminal lysine residues. The presence of the sAnk1.5 binding partner obscurin, and mutation of lysine residues increased sAnk1.5 protein levels, as did knockdown of KCTD6 in cardiomyocytes. Obscurin knockout muscle displayed reduced sAnk1.5 levels and mislocalization of the sAnk1.5/KCTD6 complex. Scaffolding functions of obscurin may therefore prevent activation of the cullin-mediated protein degradation machinery and ubiquitylation of sAnk1.5 through sequestration of sAnk1.5/KCTD6 at the sarcomeric M-band, away from the Z-disk–associated cullin-3. The interaction of KCTD6 with ankyrin-1 may have implications beyond muscle for hereditary spherocytosis, as KCTD6 is also present in erythrocytes, and erythrocyte ankyrin isoforms contain its mapped minimal binding site.
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Hu, Christine Zhiwen, Jaswinder K. Sethi, and Thilo Hagen. "The Role of the Cullin-5 E3 Ubiquitin Ligase in the Regulation of Insulin Receptor Substrate-1." Biochemistry Research International 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/282648.

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Background. SOCS proteins are known to negatively regulate insulin signaling by inhibiting insulin receptor substrate-1 (IRS1). IRS1 has been reported to be a substrate for ubiquitin-dependent proteasomal degradation. Given that SOCS proteins can function as substrate receptor subunits of Cullin-5 E3 ubiquitin ligases, we examined whether Cullin-5 dependent ubiquitination is involved in the regulation of basal IRS1 protein stability and signal-induced IRS1 degradation.Findings. Our results indicate that basal IRS1 stability varies between cell types. However, the Cullin-5 E3 ligase does not play a major role in mediating IRS1 ubiquitination under basal conditions. Protein kinase C activation triggered pronounced IRS1 destabilization. However, this effect was also independent of the function of Cullin-5 E3 ubiquitin ligases.Conclusions. In conclusion, SOCS proteins do not exert a negative regulatory effect on IRS1 by functioning as substrate receptors for Cullin-5-based E3 ubiquitin ligases both under basal conditions and when IRS1 degradation is induced by protein kinase C activation.
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van Buuren, Nick, Brianne Couturier, Yue Xiong, and Michele Barry. "Ectromelia Virus Encodes a Novel Family of F-Box Proteins That Interact with the SCF Complex." Journal of Virology 82, no. 20 (August 6, 2008): 9917–27. http://dx.doi.org/10.1128/jvi.00953-08.

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ABSTRACT Poxviruses are notorious for encoding multiple proteins that regulate cellular signaling pathways, including the ubiquitin-proteasome system. Bioinformatics indicated that ectromelia virus, the causative agent of lethal mousepox, encoded four proteins, EVM002, EVM005, EVM154, and EVM165, containing putative F-box domains. In contrast to cellular F-box proteins, the ectromelia virus proteins contain C-terminal F-box domains in conjunction with N-terminal ankyrin repeats, a combination that has not been previously reported for cellular proteins. These observations suggested that the ectromelia virus F-box proteins interact with SCF (Skp1, cullin-1, and F-box) ubiquitin ligases. We focused our studies on EVM005, since this protein had only one ortholog in cowpox virus. Using mass spectrometry, we identified cullin-1 as a binding partner for EVM005, and this interaction was confirmed by overexpression of hemagglutinin (HA)-cullin-1. During infection, Flag-EVM005 and HA-cullin-1 colocalized to distinct cellular bodies. Significantly, EVM005 coprecipitated with endogenous Skp1, cullin-1, and Roc1 and associated with conjugated ubiquitin, suggesting that EVM005 interacted with the components of a functional ubiquitin ligase. Interaction of EVM005 with cullin-1 and Skp1 was abolished upon deletion of the F-box, indicating that the F-box played a crucial role in interaction with the SCF complex. Additionally, EVM002 and EVM154 interacted with Skp1 and conjugated ubiquitin, suggesting that ectromelia virus encodes multiple F-box-containing proteins that regulate the SCF complex. Our results indicate that ectromelia virus has evolved multiple proteins that interact with the SCF complex.
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Dissertations / Theses on the topic "Cullin-1"

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Vava, Akhona. "The role of Defective in Cullin Neddylation 1 Domain Containing 1 (DCUN1D1) in prostate cancer." Master's thesis, University of Cape Town, 2014. http://hdl.handle.net/11427/6009.

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Voigt, Jana. "An improved functional screen in Xenopus identified Cullin-1 as a novel player in neurogenesis." Thesis, University of Cambridge, 2005. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.615147.

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Murray, Philip. "A clinical and molecular study of the growth disorder 3-M syndrome." Thesis, University of Manchester, 2011. https://www.research.manchester.ac.uk/portal/en/theses/a-clinical-and-molecular-study-of-the-growth-disorder-3m-syndrome(5509fea9-84a8-4883-9991-2a17d2fa4964).html.

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3-M syndrome (named after three authors who first described the condition) is an autosomal recessive condition characterised by pre- and post-natal growth impairment, facial dysmorphism and radiological features (slender long bones and tall vertebral bodies). It is caused by loss of function mutations in the Cullin 7 (CUL7) and Obscurin-like 1 (OBSL1) genes. CUL7 is a protein involved in ubiquitination (the process of targeted protein degradation) and OBSL1 is a putative cytoskeletal adaptor protein. The mechanisms through which loss of function mutations in OBSL1 or CUL7 lead to growth impairment is unclear but previous work suggests impaired placental function and altered insulin-like growth factor 1 (IGF-1) signaling as possibilities. The overall aim of this study was to elucidate the mechanisms underlying growth impairment in 3-M syndrome. Initially phenotypic data was collected on a cohort of patients and a genotype-phenotype comparison was undertaken. Skin fibroblast cell lines were derived from four patients with 3-M syndrome and used to study growth hormone (GH) and IGF-1 signal transduction, cell proliferation and apoptosis. Subsequently a hypothesis generating approach to identify novel mechanisms underlying 3-M growth impairment was undertaken in whole transcriptome and metabolomic studies. In addition an animal model using morpholino oligonucleotide mediated knock down of OBSL1 in Xenopus tropicalis was developed to study the effects on growth in a non placenting vertebrate to determine if the growth impairment seen in 3-M syndrome is independent of placental function. Cell proliferation was reduced in 3-M fibroblasts while apoptosis was not different from controls. No differences in GH signal transduction were identified but reduced activation of AKT following IGF-1 stimulation was identified in 3-M fibroblast cell lines. IGF2 was identified as the top downregulated probeset in 3-M fibroblasts compared to control in the whole genome transcriptome analysis. Metabolomic changes related to energy metabolism were identified in 3-M syndrome fibroblasts. Knock down of xtOBSL1 using two independent morpholinos resulted in growth impairment at embryonic stage 50, suggesting the growth impairment seen is at least in part independent of placental function. These studies suggest impaired placental function is not a key component of the growth impairment in 3-M syndrome. Impairment of IGF-1 signal transduction and IGF2 silencing are likely to contribute to the growth impairment in 3-M syndrome. The mechanisms relating to this IGF2 silencing require further studies.
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Salon, Caroline. "Contribution d'une dérégulation de l'expression du facteur de transcription E2F1 à la carcinogenèse bronchopulmonaire." Université Joseph Fourier (Grenoble), 2007. http://www.theses.fr/2007GRE10105.

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Le facteur de transcription E2F1 joue un rôle crucial dans le contrôle de la croissance cellulaire et de l'apoptose et peut exercer, soit des propriétés oncogéniques, soit des propriétés suppressives de tumeur. Ayant préalablement décrit son profil d'expression différentielle dans les tumeurs bronchiques, nous avons étudié son rôle potentiel dans ces tumeurs. Nous montrons que E2FI restaure l'apoptose dans des cellules d'adénocarcinomes pulmonaires en inhibant l'expression de l'isoforme courte du facteur antiapoptotique c-FLIP, résultant en une activation de la caspase-8. De plus, nous montrons que E2F 1 sensibilise les cellules tumorales à la mort induite par les ligands de mort F ASL et TRAIL et aux effets cytotoxiques de lymphocytes T activés. Ces résultats suggèrent que de bas niveaux d'expression de E2FI contribuent à la progression tumorale des adénocarcinomes pulmonaires par échappement à l'apoptose et à la réponse immune anti-tumorale. Le complexe SCFSKP2 appartient à la famille des ubiquitine-E3 ligases et a été impliqué dans la protéolyse dépendante du protéasome de E2F 1. Il comprend entre autres la protéine à domaine Fbox, SKP2, et la protéine de structure culline1. Nous avons mis en évidence l'existence d'une coopération oncogénique entre E2FI et SKP2 pour activer la transcription du gène de croissance cellulaire cycline E dans des tumeurs neuroendocrines pulmonaires de haut grade de malignité. De plus, nous décrivons pour la première fois une dérégulation de l'expression et/ou de la neddylation de culline-I dans les carcinomes pulmonaires et suggérons un rôle de cette protéine dans le contrôle du niveau d'expression protéique de cycline E
The transcription factor E2FI plays a crucial role in the control of cellular growth and apoptosis, and also exerts oncogenic or tumor suppressive properties. Having established a differential pattern of its protein expression in lung tumors, we have studied its potential role in these tumors. We show that E2F 1 restores the apoptosis of various lung adenocarcinoma celllines by inhibiting the expression of the short isoform of the anti-apoptotic protein c-FLIP, leading to the activation of caspase-8. Moreover, we demonstrate that E2F 1 can sensitize the se cells to the death induced by death receptors ligands, such as Fas or TRAIL, as well as to the cytotoxicity mediated by activated T lymphocytes. Therefore, these results identify a new cellular pathway by which E2F 1 induces apoptosis. Moreover they suggest that the low level of E2F 1 protein detected in lung adenocarcinomas might contribute to their tumoral progression by enabling the escape oftumor cells to apoptosis, as weIl as to the antitumoral immune response. The SCFSKP2 complex belongs to a family of E3 ubiquitin ligases and was previously involved in the proteolysis of E2FI mediated by proteasome. SCFSKP2 complexes contain the F. Box protein SKP2 and the scaffold protein Collin-l. We provide evidence of an oncogenic cooperation between SKP2 and E2FI proteins in high grade neuroendocrine lung carcinomas, involving the transcriptional activation of cyclin E, a major cell cycle regulator. Moreover, we describe for the fust time an altered pattern of Cu1lin- 1 protein expression and/or neddylation in lung carcinomas, and we suggest a role of Cullin-l in the control of Cyclin E protein expression
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Bosu, Dimple R. "CAND-1 and regulation of cullin RING ubiquitin ligases in C. elegans." 2008. http://purl.galileo.usg.edu/uga%5Fetd/bosu%5Fdimple%5Fr%5F200812%5Fphd.

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Kim, Jihyun. "The function of CUL-4 ubiquitin ligase complexes in DNA replication and enhancers of cullin-inhibitor CAND-1 in C. elegans." 2009. http://purl.galileo.usg.edu/uga%5Fetd/kim%5Fjihyun%5F200905%5Fphd.

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Reichermeier, Kurt Michael. "Quantitative Characterization of Composition and Regulation of Cullin-RING Ubiquitin Ligases." Thesis, 2020. https://thesis.library.caltech.edu/13606/1/Caltech_Thesis_Reichermeier_v10_proof.pdf.

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Induced proteolysis of pathogenic proteins via degrader molecules, such as Proteolysis Targeting Chimeras (PROTACs), is emerging as a promising therapeutic strategy. In particular, induced proximity of Cullin-RING ubiquitin Ligases (CRLs) with various neo-substrates has proven successful in mediating proteasomal degradation of previously undruggable proteins. Hijacking enzymes to carry out biochemical reactions on neo-substrates stands in stark contrast to conventional pharmacological approaches and exposes degrader molecules to unusually complex pharmacodynamics. While the first PROTACs entered the clinic in 2019, much about the organization and regulation of the frequently co-opted CRLs remains elusive. In particular, the COP9 Signalosome (CSN) is essential to regulate CRL activity and assembly through cleaving Nedd8 from cullin scaffolds, yet it remains unknown how CSN becomes activated. We combine structural and kinetic analyses to identify mechanisms that contribute to CSN activation and Nedd8 deconjugation, detailing the kinetic picture of the deneddylation-disassembly cycle that promotes rapid remodeling of the cellular CRL network. Furthermore, we establish Protein Interaction Kinetics and Estimation of Stoichiometries (PIKES) analysis, a systematic proteomic profiling platform that integrates cellular engineering, affinity purification, chemical stabilization and quantitative mass spectrometry to investigate the dynamics of interchangeable multiprotein complexes. Using PIKES, we show that ligase assemblies of Cullin4 with individual substrate receptors differ in abundance by up to 200-fold and that Cand1 acts as an exchange factor to remodel the CRL4 ligase pool. Integrating quantitative data and model simulations of CRL-mediated substrate turnover, we show that high substrate receptor levels can enhance the potency of degraders.
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Mosadeghi, Ruzbeh. "Mechanistic Dissection of the Cop9 Signalosome’s Deneddylation Activity on Cullin-RING Ligases." Thesis, 2015. https://thesis.library.caltech.edu/8951/1/06122015%20Ruzbeh%20Mosadeghi%20Thesis.pdf.

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We set out to understand the precise mechanisms that regulate the activation and deactivation of Cullin-RING Ligases (CRLs). While a great deal of work has already gone into identifying the players involved in these pathways and the cellular consequences associated with the loss of each, the biochemical mechanisms regulating these steps have remained elusive. In this work we sought to gain a better understanding of the mechanisms behind these steps by teasing apart specific their biochemical reactions. By measuring the individual microscopic rate constants of the reactions we have shed light on both the proper sequence of events in the regulation of CRLs as well as how they are in fact controlled.

Prior to this work, it was believed that CSN deactivated CRLs by binding them and enzymatically removing the activating post-translation modification Nedd8. It was believed that CSN could not bind to CRLs while they were active due to the steric hindrance by the CRL substrates, and that they would remain bound to deneddylated CRLs as a sequestering agent until a new substrate could displace it. We now have some insight that substrates themselves cannot inhibit CSN very well, but that the active ubiquitination by an E2 enzyme precludes CSN binding and activity. When the substrate for a CRL becomes depleted, CSN then binds to the CRL in a low affinity, low activity conformation. This triggers a conformational change that pulls the autoinhibitory Ins-1 loop away from the active site in the catalytic subunit Csn5, resulting in a large increase in affinity and cleavage of the isopeptide bond between CRLs and Nedd8. Upon dissociation of Nedd8, CSN rapidly returns to the low affinity state and dissociates from the CRL, allowing it reenter its activation cycle.

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Christmann, Martin. "Deneddylation and fungal development - Regulation of Nedd8 protein modification by DenA and the COP9 signalosome." Doctoral thesis, 2011. http://hdl.handle.net/11858/00-1735-0000-000D-EF70-1.

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Books on the topic "Cullin-1"

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Wentworth, Tricia. The Culling: Book 1. Independently published, 2017.

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Howe, Angela. Culling and Atonement: Depopulation Books 1 And 2. Independently Published, 2019.

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Food and Rural Affairs Committee Great Britain: Parliament: House of Commons: Environment and Michael Jäck. Bovine TB : Badger culling, sixth report of session 2005-06, Vol. 1: Report, together with formal minutes and lists of oral and written Evidence. Stationery Office, The, 2006.

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Book chapters on the topic "Cullin-1"

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Zhang, Hui. "Cullin Ubiquitin E3 Ligases." In Encyclopedia of Cancer, 1–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27841-9_7191-1.

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Deshaies, Raymond J., Ethan D. Emberley, and Anjanabha Saha. "Control of Cullin-Ring Ubiquitin Ligase Activity by Nedd8." In Subcellular Biochemistry, 41–56. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6676-6_4.

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Franciosini, Anna, and Giovanna Serino. "Immunoprecipitation of Cullin-RING Ligases (CRLs) in Arabidopsis thaliana Seedlings." In Methods in Molecular Biology, 11–21. New York, NY: Springer New York, 2016. http://dx.doi.org/10.1007/978-1-4939-3759-2_2.

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Casagrande, Federica, and Giovanna Serino. "Immunoprecipitation of Cullin–Ring Ligases (CRLs) in Arabidopsis thaliana Seedlings." In Methods in Molecular Biology, 31–42. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2784-6_3.

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Yamoah, Kosj, Kenneth Wu, and Zhen‐Qiang Pan. "In Vitro Cleavage of Nedd8 from Cullin 1 by COP9 Signalosome and Deneddylase 1." In Methods in Enzymology, 509–22. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)98042-7.

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"Cullin (CUL1)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 449. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_3919.

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"CDC53 (cullin, CUL)." In Encyclopedia of Genetics, Genomics, Proteomics and Informatics, 292. Dordrecht: Springer Netherlands, 2008. http://dx.doi.org/10.1007/978-1-4020-6754-9_2573.

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"1: Compute-Based Tiled Culling." In GPU Pro 6, 453–76. A K Peters/CRC Press, 2015. http://dx.doi.org/10.1201/b18805-31.

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Conference papers on the topic "Cullin-1"

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Pikor, Larissa, Kelsie L. Thu, William W. Lockwood, Raj Chari, Ian M. Wilson, Calum E. MacAulay, John C. English, et al. "Abstract A14: DNA alterations to the Cullin-3/Ring box protein-1 E3 ubiquitin ligase complex represent a novel mechanism of NF-κB activation in lung cancer." In Abstracts: AACR International Conference on Frontiers in Cancer Prevention Research‐‐ Nov 7-10, 2010; Philadelphia, PA. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1940-6207.prev-10-a14.

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Li, Xuesen, Zhongbo Liu, Shuman Liu, Xia Xu, Zheng Sun, Christopher A. Blair, Anne R. Simoneau, and Xiaolin Zi. "Abstract 857: Flavokawains degrade S-phase kinase-associated protein 2 (Skp2) via deneddylation of cullin-1 and inhibit prostate cancer in the transgenic adenocarcinoma of the mouse prostate (TRAMP) model." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-857.

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Freitag, Lori, and Tim Urness. "Analyzing Industrial Furnace Efficiency Using Comparative Visualization in a Virtual Reality Environment." In ASME 1999 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 1999. http://dx.doi.org/10.1115/imece1999-0174.

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Abstract:
Abstract We describe an interactive toolkit used to perform comparative analysis of two or more data sets arising from numerical simulations. Several techniques have been incorporated into this toolkit, including (1) successive visualization of individual data sets, (2) data comparison techniques such as computation and visualization of the differences between data sets, and (3) image comparison methods such as scalar field height profiles plotted in a common coordinate system. We describe each technique in detail and show example usage in an industrial application aimed at designing an efficient, low-NOx burner for industrial furnaces. Critical insights are obtained by interactively adjusted color maps, data culling, and data manipulation. New paradigms for scaling small values in the data comparison technique are described. The display device used for this application was the CAVE virtual reality theater, and we describe the user interface to the visualization toolkit and the benefits of immersive 3D visualization for comparative analysis.
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