Search results for "SUMO protein"

showing 10 items of 11 documents

Lack of NFATc1 SUMOylation prevents autoimmunity and alloreactivity

2020

A novel transgenic mouse, in which the transcription factor NFATc1 bears lysine-to-arginine mutations that prevent modification by SUMO, develops normally and is healthy. However, SUMO-insensitive NFATc1 transmits strong tolerogenic signals, thus preventing autoimmune and alloimmune T cell responses.

0301 basic medicineProtein sumoylationEncephalomyelitis Autoimmune ExperimentalT cellStem Cells & RegenerationImmunologySUMO proteinAutoimmunityBiologyenvironment and public healthT-Lymphocytes RegulatoryArticleMinor Histocompatibility AntigensMice03 medical and health sciences0302 clinical medicineImmune systemNeuroinflammationAldesleukinSTAT5 Transcription FactormedicineAnimalsImmunology and AllergyTranscription factorMice Knockoutintegumentary systemNFATC Transcription FactorsExperimental autoimmune encephalomyelitisSumoylationNFATmedicine.diseaseCell biologyenzymes and coenzymes (carbohydrates)030104 developmental biologymedicine.anatomical_structureProto-Oncogene Proteins c-bcl-2030220 oncology & carcinogenesisCytokinesPositive Regulatory Domain I-Binding Factor 1Journal of Experimental Medicine
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Functions of SETD7 during development, homeostasis and cancer

2019

A controlled organ homeostasis is essential to sustain the integrity of any living organism. This homeostasis relies on stem cells, which maintain themselves and give rise to the various types of differentiated cells. It is well established that the differentiation of pluripotent embryonic stem cells (ESCs) depends on major changes in transcriptional programs. Covalent modifications of DNA, RNA and proteins are instrumental in setting up the genetic programs associated with cell fates. Another important mechanism for regulation of gene expression is protein localisation and stability. In addition to ubiquitination, SUMOylation and phosphorylation, methylation of proteins is an important det…

0301 basic medicineRegulation of gene expressionCellular differentiationCellSUMO proteinRNABiologyEmbryonic stem cellCell biology03 medical and health sciencesEditorial Commentary030104 developmental biology0302 clinical medicinemedicine.anatomical_structure030220 oncology & carcinogenesismedicineStem cellOrganism
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Arabidopsis TCP Transcription Factors Interact with the SUMO Conjugating Machinery in Nuclear Foci

2017

In Arabidopsis more than 400 proteins have been identified as SUMO targets, both in vivo and in vitro. Among others, transcription factors (TFs) are common targets for SUMO conjugation. Here we aimed to exhaustively screen for TFs that interact with the SUMO machinery using an arrayed yeast two-hybrid library containing more than 1,100 TFs. We identified 76 interactors that foremost interact with the SUMO conjugation enzyme SCE1 and/or the SUMO E3 ligase SIZ1. These interactors belong to various TF families, which control a wide range of processes in plant development and stress signaling. Amongst these interactors, the TCP family was overrepresented with several TCPs interacting with diffe…

0301 basic medicineyeast two-hybridTwo-hybrid screeninggenetic processesSUMO proteinLaboratory of VirologyPlant Sciencemacromolecular substanceslcsh:Plant cultureenvironment and public healthLaboratorium voor Virologie03 medical and health sciencesArabidopsistranscription factorsTranscription factorslcsh:SB1-1110Transcription factorOriginal ResearchGeneticschemistry.chemical_classificationbiologySUMO conjugationChemistryYeast two-hybridbiology.organism_classificationIn vitroYeastCell biologyUbiquitin ligaseenzymes and coenzymes (carbohydrates)030104 developmental biologyEnzymeSUMObiology.proteinhealth occupationsEPSTCP
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Sumoylation of the transcription factor NFATc1 leads to its subnuclear relocalization and interleukin-2 repression by histone deacetylase.

2009

The family of NFAT (nuclear factor of activated T-cells) transcription factors plays an important role in cytokine gene regulation. In peripheral T-cells NFATc1 and -c2 are predominantly expressed. Because of different promoter and poly(A) site usage as well as alternative splicing events, NFATc1 is synthesized in multiple isoforms. The highly inducible NFATc1/A contains a relatively short C terminus, whereas the longer, constitutively expressed isoform NFATc1/C spans an extra C-terminal peptide of 246 amino acids. Interestingly, this NFATc1/C-specific terminus can be highly sumoylated. Upon sumoylation, NFATc1/C, but not the unsumoylated NFATc1/A, translocates to promyelocytic leukemia nuc…

Gene isoformSUMO proteinBiologyBiochemistryHistone DeacetylasesCell LineMiceAnimalsHumansProtein IsoformsMolecular BiologyTranscription factorRegulation of gene expressionCell NucleusLymphokinesintegumentary systemNFATC Transcription FactorsActivator (genetics)Mechanisms of Signal TransductionNFATCell BiologyMolecular biologyChromatinHistoneGene Expression RegulationUbiquitin-Conjugating Enzymesbiology.proteinSmall Ubiquitin-Related Modifier ProteinsInterleukin-2Histone deacetylaseThe Journal of biological chemistry
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An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16

2014

Summary Human papillomaviruses (HPV) induce warts and cancers on skin and mucosa. The HPV16 capsid is composed of the proteins L1 and L2. After cell entry and virus disassembly, the L2 protein accompanies the viral DNA to promyelocytic leukaemia nuclear bodies (PML-NBs) within the host nuclei enabling viral transcription and replication. Multiple components of PML-NBs are regulated by small ubiquitin-like modifiers (SUMOs) either based on covalent SUMO modification (SUMOylation), or based on non-covalent SUMO interaction via SUMO interacting motifs (SIMs). We show here that the HPV16 L2 comprises at least one SIM, which is crucial for the L2 interaction with SUMO2 in immunoprecipitation and…

ImmunoprecipitationvirusesImmunologyMutantSUMO proteinvirus diseasesColocalizationSUMO2BiologyMicrobiologyMolecular biologyVirusCapsidTranscription (biology)Virologyembryonic structuresCellular Microbiology
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SUMOylation of Blimp-1 promotes its proteasomal degradation

2011

Abstract B lymphocyte induced maturation protein-1 (Blimp-1) is a transcription repressor of the Krueppel-like family. Blimp-1 plays important roles in developmental processes, such as of germ cells and hair follicle stem cells. In B lymphocytes Blimp-1 orchestrates the terminal differentiation into plasma cells. We discovered that Blimp-1 undergoes SUMOylation by SUMO-1. This SUMOylation is modulated by the SUMO protease SENP1. While Blimp-1 is relatively stable in 293T cells, a fusion with SUMO1 rendered it to rapid proteasomal degradation. Increase in SENP1 activity stabilized Blimp-1, while a decrease promoted its degradation. Our data indicate that SUMOylation of Blimp-1 regulates its …

Proteasome Endopeptidase ComplexSENP1ImmunoprecipitationSUMO-1 ProteinBiophysicsSUMO proteinPlasma cellPlasma cellBiologyBiochemistryCell LineProtein–protein interactionSENP1Structural BiologyEndopeptidasesGeneticsmedicineHumansMolecular BiologyProteasomeProtein StabilityHEK 293 cellsSumoylationCell BiologyCell biologyRepressor ProteinsCysteine Endopeptidasesmedicine.anatomical_structureProteasomeSUMO proteasePositive Regulatory Domain I-Binding Factor 1IntracellularFEBS Letters
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Heat shock protein 27 is involved in SUMO-2/3 modification of heat shock factor 1 and thereby modulates the transcription factor activity

2009

Heat shock protein 27 (HSP27) accumulates in stressed cells and helps them to survive adverse conditions. We have already shown that HSP27 has a function in the ubiquitination process that is modulated by its oligomerization/phosphorylation status. Here, we show that HSP27 is also involved in protein sumoylation, a ubiquitination-related process. HSP27 increases the number of cell proteins modified by small ubiquitin-like modifier (SUMO)-2/3 but this effect shows some selectivity as it neither affects all proteins nor concerns SUMO-1. Moreover, no such alteration in SUMO-2/3 conjugation is achievable by another HSP, such as HSP70. Heat shock factor 1 (HSF1), a transcription factor responsib…

Protein sumoylationTranscriptional ActivationCancer Researchendocrine systemanimal structuresSUMO proteinHSP27 Heat-Shock ProteinsBiologyurologic and male genital diseasesenvironment and public healthSubstrate Specificity03 medical and health sciencesTransactivation0302 clinical medicineHeat Shock Transcription FactorsHeat shock proteinGeneticsAnimalsHumansAnimals Cell Nucleus/metabolism DNA-Binding Proteins/*metabolism HSP27 Heat-Shock Proteins/chemistry/*metabolism Hela Cells Humans Protein Multimerization Protein Structure[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyHSF1Protein Structure QuaternaryMolecular BiologyTranscription factorUbiquitinsHeat-Shock Proteins030304 developmental biologyCell Nucleus0303 health sciencesMolecular biologyHsp70Cell biologyHeat shock factorDNA-Binding ProteinsProtein TransportQuaternary Protein Transport Small Ubiquitin-Related Modifier Proteins/*metabolism Substrate Specificity Transcription Factors/*metabolism Transcriptional Activation Ubiquitins/*metabolism030220 oncology & carcinogenesisembryonic structuresSmall Ubiquitin-Related Modifier ProteinsProtein MultimerizationHeLa CellsMolecular ChaperonesTranscription Factors
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Coordinated Sumoylation and Ubiquitination Modulate EGF Induced EGR1 Expression and Stability

2011

Background Human early growth response-1 (EGR1) is a member of the zing-finger family of transcription factors induced by a range of molecular and environmental stimuli including epidermal growth factor (EGF). In a recently published paper we demonstrated that integrin/EGFR cross-talk was required for Egr1 expression through activation of the Erk1/2 and PI3K/Akt/Forkhead pathways. EGR1 activity and stability can be influenced by many different post-translational modifications such as acetylation, phosphorylation, ubiquitination and the recently discovered sumoylation. The aim of this work was to assess the influence of sumoylation on EGF induced Egr1 expression and/or stability. Methods We …

Time FactorsTranscription GeneticSUMO proteinlcsh:MedicineUbiquitin-conjugating enzymeBiochemistrychemistry.chemical_compoundEpidermal growth factorMG132protein 1lcsh:ScienceMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3MultidisciplinaryProtein translationProtein Stabilitygene expression regulationCell biologyepidermal growth factorResearch Articlemedicine.drugProteasome Endopeptidase Complexendocrine systemkinase 1SUMO-1 ProteinBiologyDNA-binding proteinsGeneticsmedicineHumansBiologySettore BIO/10 - BIOCHIMICAProtein kinase BPI3K/AKT/mTOR pathwayEarly Growth Response Protein 1lcsh:RMitogen-activated proteinProteinsSumoylationRegulatory proteinsenzyme activationRNA stabilityMolecular biologychemistryProteolysisUbiquitin-Conjugating EnzymesProteasome inhibitorlcsh:QEarly growth responseGene expressionCell linePLoS ONE
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Post-translational Modifications in Plant Nuclear Signaling: Novel Insights Into Responses to Environmental Changes

2019

Just imagine a Plant Science professor in front of a classroom full of interested and attentive students. Imagine what their answers to this intriguing question would be: “What are, according to you, the functions ensured by the plant cell nucleus?” It would be very surprising if some of them would answer cell signaling in response to biotic and abiotic stresses or developmental processes. Most of them would probably answer according to a classical point of view: DNA replication or gene expression. Hence it is still admitted in recent publications (see for instance Fedorenko et al., 2010) that molecules smaller than 40 kDa can diffuse freely across the nuclear envelope pores. However, Pauly…

[SDV]Life Sciences [q-bio]SUMO proteinPlant Sciencelcsh:Plant culture03 medical and health sciences0404 agricultural biotechnologynucleus;post-translation modification (PTM);phosphorylation;acetylation;SUMOylationpost-translation modification (PTM)medicine[SDV.BV]Life Sciences [q-bio]/Vegetal Biologylcsh:SB1-1110030304 developmental biologyacetylation0303 health sciencesChemistryphosphorylationnucleus04 agricultural and veterinary sciences040401 food scienceSUMOylationCell biologymedicine.anatomical_structureEditorialAcetylation[SDE]Environmental SciencesPosttranslational modificationPhosphorylationAcetylation ; Nucleus ; Phosphorylation ; Post-translation Modification (ptm) ; SumoylationNucleusFrontiers in Plant Science
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Thyroid hormones induce sumoylation of the cold shock domain-containing protein PIPPin in developing rat brain and in cultured neurons.

2006

We previously identified a cold shock domain (CSD)-containing protein (PIPPin), expressed at high level in brain cells. PIPPin has the potential to undergo different post-translational modifications and might be a good candidate to regulate the synthesis of specific proteins in response to extracellular stimuli. Here we report the effects of thyroid hormone (T3) on PIPPin expression in developing rat brain. We found that a significant difference among euthyroid- and hypothyroid- newborn rats concerns sumoylation of nuclear PIPPin, that is abolished by hypothyroidism. Moreover, T3-dependence of PIPPin sumoylation has been confirmed in cortical neurons purified from brain cortices and culture…

medicine.medical_specialtySUMO-1 ProteinSUMO proteinDeveloping rat brainNerve Tissue ProteinsEndocrinologyAntithyroid AgentsHypothyroidismPregnancyInternal medicinemedicineExtracellularAnimalsRats WistarCells CulturedCell NucleusCerebral CortexNeuronsbiologyRNA-Binding ProteinsCold-shock domainChromatinProtein Structure TertiaryRatsThyroid hormoneChemically defined mediumCell nucleusmedicine.anatomical_structureHistoneEndocrinologyAnimals NewbornPropylthiouracilPrenatal Exposure Delayed Effectsbiology.proteinTriiodothyronineRNA-binding proteins (RBPs)FemaleRabbitsNucleusEndocrinology
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