AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth Care
Endoplasmic ReticulumEndoplasmic Reticulum StressEndoplasmic Reticulum, RoughSarcoplasmic ReticulumEndoplasmic Reticulum, SmoothGolgi ApparatusUnfolded Protein ResponseProtein TransportMembrane ProteinsMolecular Sequence DataMolecular ChaperonesProteasome Endopeptidase ComplexAmino Acid SequenceCell LineCalciumTunicamycinIntracellular MembranesSarcoplasmic Reticulum Calcium-Transporting ATPasesTranscription Factor CHOPCalnexinProtein FoldingCalcium-Transporting ATPasesCalreticulinThapsigarginBrefeldin AProtein Processing, Post-TranslationalMutationMicroscopy, ElectronCell MembraneGlycosylationBiological TransportMicrosomesActivating Transcription Factor 6Heat-Shock ProteinsCells, CulturedProtein BindingEndoplasmic Reticulum-Associated DegradationProtein Sorting SignalsUbiquitinProteolysisCaspase 12KineticsSubcellular FractionsCOP-Coated VesiclesCytosolModels, BiologicalProtein Structure, TertiaryHeLa CellsSignal TransductionProtein Disulfide-IsomerasesStress, PhysiologicalRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsApoptosisCOS CellsCricetinaeCytoplasmCalcium-Binding ProteinsCalcium SignalingMicroscopy, FluorescenceBase SequenceCarrier ProteinsRNA, MessengerLiverBlotting, WesternUbiquitinationUbiquitin-Protein LigasesCysteine EndopeptidasesMitochondriaRabbitsCell FractionationCercopithecus aethiopsTransfectionTime FactorsVesicular Transport ProteinsCell CompartmentationMicroscopy, ConfocalProtein BiosynthesisCHO CellsInositol 1,4,5-Trisphosphate ReceptorsGlycoproteinsPhosphorylationSequence Homology, Amino AcidProteinsCell Line, TumorMultienzyme ComplexesRecombinant ProteinsMembrane GlycoproteinsGreen Fluorescent ProteinsAutophagyActivating Transcription Factor 4Biodegradation, EnvironmentalHSP70 Heat-Shock ProteinsHEK293 CellsAdenosine TriphosphateImmunoblottingeIF-2 KinaseFungal ProteinsHydrolysis
Boosting the unfolded proteinNucleic acidsTransmembraneSynthesisLumenExtracellular matrixCellular proteinsERADHomeostasisTranscription factorsModulationEnzymesMechanismPost-translationaAutophagyAccumulationComplexesAffinityReducesImmuneRegulatoryBindCompartmentsNucleusResponseDiseasesSecretory pathwayGeneStressOccurPlasmaActivationControlFunctionsSubjectCellsBroad rangeCellSpecificRoleType
Boosting the unfolded protein1
  • Recent research of the lab on cellular and mouse models of Huntington's disease has led to the discovery of a promising therapeutic approach to the disease, boosting the unfolded protein response. (tau.ac.il)
Nucleic acids2
  • PDT cytotoxic properties have been established to be due to the oxidation of a large range of biomolecules in cells, including nucleic acids, lipids, and proteins, leading to severe alteration in cell signaling cascades or in gene expression regulation [ 13 , 14 ] . (oaepublish.com)
  • Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus. (lookformedical.com)
Transmembrane4
  • Phosphorylation enhances FAM134B oligomerization and its activity in membrane fragmentation and ER-phagy To understand how FAM134B oligomerization was increased under autophagy-stimulating or ER-stress conditions, we conducted mass Figure 1.Here, we identified that the endoplasmic reticulum (ER)-located transmembrane selenoprotein K (SELENOK) was induced during virus infection and facilitated innate immune responses against herpes simplex virus-1 (HSV-1). (baumaschinen-knell.de)
  • Ceramide generated in late endosomal compartments is recognized as a potent regulator of cell signaling, but its molecular interactions with late endosomal transmembrane proteins have not been studied in depth. (sphingolipidclub.com)
  • Here we uncover structural motifs required for ceramide interaction with the four membrane spanning Lysosome Associated Protein Transmembrane 4B (LAPTM4B). (sphingolipidclub.com)
  • Wolfram syndrome type 1 gene ( WFS1 ), which encodes a transmembrane structural protein (wolframin), is essential for several biological processes, including proper inner ear function. (biomedcentral.com)
Synthesis4
  • The UPR activation involves three major downstream effects including reduction in protein synthesis to reduce ER load, enhancement of ER protein folding capacity and upregulation of ER-associated protein degradation (ERAD). (distantreader.org)
  • Membrane traffic is a fundamental process by which a third of the mammalian proteins are transported from their site of synthesis, the endoplasmic reticulum (ER), through a series of anatomically separated membranous compartments until they reach their cellular destinations in correctly processed forms. (oncotarget.com)
  • The proteostasis network (PN) is an assembly of distinct dynamic molecular pathways that control the functionality of the proteome (proteome homeodynamics) during protein synthesis, folding, trafficking, and degradation. (hindawi.com)
  • For instance, the association of mitochondria with the endoplasmic reticulum (ER), in a juxtaposition known as Mitochondria-Associated Membrane (MAM), has an important role in controlling mitochondria biogenesis, Ca 2+ release, and lipid synthesis and apoptosis [ 10 , 11 ]. (hindawi.com)
Lumen3
  • One of these PTMs, Nε-lysine acetylation, was thought to occur only in the mitochondria, cytosol and nucleus, but this paradigm was challenged in the past decade with the discovery of lysine acetylation in the lumen of the endoplasmic reticulum (ER). (biologists.com)
  • ER stress arises from conditions that cause the accumulation of misfolded or unfolded proteins within the ER lumen. (biomedcentral.com)
  • Once protein is translated by ERassociated ribosomes, it enters into the ER lumen and is folded in a chaperon-assisted manner. (distantreader.org)
Extracellular matrix2
  • TG2 is also found in the extracellular space where it functions in protein cross-linking and extracellular matrix stabilization. (bvsalud.org)
  • Given the central role of Src in extracellular matrix (ECM) degradation, we investigated the impact of the KDELR-Src pathway on the ability of cancer cells to degrade the ECM. (oncotarget.com)
Cellular proteins2
  • Thus, TG2 performs a multitude of functions in multiple cellular compartments making it one of the most versatile cellular proteins. (bvsalud.org)
  • A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. (lookformedical.com)
ERAD4
  • He has focused especially on mechanisms of ER quality control of protein folding and on recognition and delivery of misfolded proteins from the ER to the cytosolic proteasomes for ERAD. (tau.ac.il)
  • Delivery of misfolded proteins to ER-associated degradation (ERAD). (tau.ac.il)
  • These processes are regulated by ER stress and the consequent unfolded protein response (UPR) and he has established that the compartmentalization and assembly of a molecular complex that targets to ERAD are dependent on one of the branches of the UPR. (tau.ac.il)
  • His group has found that interference with ERAD and upregulation of the UPR are a main mechanism of cell damage in a neurodegenerative disorder, Huntington's disease, and that this occurs prior to the appearance of the characteristic large protein inclusions that occur in this disease. (tau.ac.il)
Homeostasis5
  • Protein post-translational modifications (PTMs) take many shapes, have many effects and are necessary for cellular homeostasis. (biologists.com)
  • This Review summarizes the more recent biochemical, cellular and mouse model studies that underscore the importance of the ER acetylation process in maintaining protein homeostasis and autophagy within the secretory pathway, and its impact on developmental and age-associated diseases. (biologists.com)
  • ER stress induces activation of the unfolded protein response (UPR), a signaling network that is required to resolve stress, restoring ER homeostasis and promoting cell survival and adaptation. (biomedcentral.com)
  • Of particular importance in transglutaminase research are recent findings concerning the role of TG2 in gene expression, protein homeostasis, cell signaling, autoimmunity, inflammation, and hypoxia. (bvsalud.org)
  • Despite the stringent regulation around protein folding and redundancy within the chaperone-assisted folding process, both endogenous and exogenous triggers can disrupt the ER homeostasis and increase protein misfolding. (distantreader.org)
Transcription factors2
Modulation2
Enzymes2
  • This spliced form of XBP1 then translates into a transcription factor, which further translocates into the nucleus where it induces expression of a wide variety of genes including ER-associated chaperones and protein folding enzymes to increase ER size and folding capacity. (distantreader.org)
  • The mitochondria have their own chaperones and proteolytic enzymes that remove damaged or unfolded proteins [ 18 - 20 ]. (hindawi.com)
Mechanism1
  • The control of nuclear localization via phosphorylation and dephosphorylation serves as the primary regulatory mechanism for MiT family proteins, and several kinases and phosphatases have been identified to directly determine the transcriptional activities of MiT proteins. (molcells.org)
Post-translationa1
Autophagy1
Accumulation1
  • Ageing leads to a gradual dysfunction of the proteostasis network and thus to proteome instability due to accumulation of damaged and/or misfolded proteins [ 2 ]. (hindawi.com)
Complexes2
  • The 48 kDa subunit, RETINOBLASTOMA-BINDING PROTEIN 4, is also a component of several other protein complexes involved in chromatin remodeling. (lookformedical.com)
  • It is found as a subunit of protein complexes that are in involved in the enzymatic modification of histones including the Mi2 and Sin3 histone deacetylase complexes and the polycomb repressive complex 2. (lookformedical.com)
Affinity3
  • GRP78 has a high affinity for misfolded and unfolded proteins: when luminal load of misfolded protein increases, GRP78 is released from the ER stress sensors, which are then free to initiate downstream signalling outside the ER. (distantreader.org)
  • Although initially discovered as a retinoblastoma binding protein it has an affinity for core HISTONES and is a subunit of chromatin assembly factor-1 and polycomb repressive complex 2. (lookformedical.com)
  • A retinoblastoma-binding protein that has an affinity for core HISTONES. (lookformedical.com)
Reduces1
  • Modification of protein bound glutamines reduces ubiquitin-dependent proteasomal degradation. (bvsalud.org)
Immune1
Regulatory2
Bind2
Compartments1
  • Tissue transglutaminase (TG2) is a widely distributed multifunctional protein involved in a broad range of cellular and metabolic functions carried out in a variety of cellular compartments. (bvsalud.org)
Nucleus2
Response3
  • The misfolding hypothesis suggests that slow folding during HLA-B27's tertiary structure folding and association with β2 microglobulin causes the protein to be misfolded, therefore initiating the unfolded protein response (UPR)-a pro-inflammatory endoplasmic reticulum (ER) stress response. (wikipedia.org)
  • Spliced X-box binding protein-1 (XBP1s) is a protein that belongs to the cAMP-response element-binding (CREB)/activating transcription factor (ATF) b-ZIP family with a basic-region leucine zipper (bZIP). (mdpi.com)
  • When protein secretion demand exceeds the protein folding capacity of the ER, the unfolded protein response (UPR) is triggered as a consequence of ER stress. (distantreader.org)
Diseases1
  • Protein misfolding diseases, focusing on neurodegenerative diseases, especially Huntington's disease. (tau.ac.il)
Secretory pathway1
Gene1
  • This includes gene, protein and metabolic networks, cellular architecture and intracellular dynamics, cell communication and motility, cell division and differentiation, tissue formation and organogenesis, tissue and organ functions, changes in population characteristics as a consequence of interaction of organisms with their physical environment, with individuals of their own species, and with organisms of other species. (nih.gov)
Stress5
  • Protein misfolding and ER stress in Huntington's disease. (tau.ac.il)
  • In the present study we examined the protective potential of exogenously administered human umbilical cord derived mesenchymal stem cells (UCMSCs) against Dextran Sulfate Sodium (DSS) induced acute colitis in immunodeficient NOD.CB 17 - Prkdc scid /J mice with particular attention to endoplasmic reticulum (ER) stress. (biomedcentral.com)
  • Moreover, colon length, histological changes, myeloperoxidase and catalase activities, metalloproteinase (MMP) 2 and 9 expression and endoplasmic reticulum (ER) stress related proteins were evaluated on day 7. (biomedcentral.com)
  • The epithelial cells of the gastrointestinal tract, because of their barrier function, are exposed to toxins and infectious agents that can adversely affect protein folding in the ER and cause ER stress. (biomedcentral.com)
  • Aggregated misfolded proteins in the ER cause cellular stress, which if unresolved can lead to cell death. (distantreader.org)
Occur1
  • Additional complex modifications occur before the protein is transported to Golgi. (distantreader.org)
Plasma1
Activation2
  • The dissociation of GRP78 allows IRE1 dimerisation and activation of C-terminal endoribonuclease activity, which non-canonically splices a 26-base pair intron from the X-box binding protein 1 (XBP1) mRNA to produce the spliced form of XBP1 (sXBP1). (distantreader.org)
  • The KDELR induces Src activation at the invadopodia and leads to phosphorylation of the Src substrates cortactin and ASAP1, which are required for basal and KDELR-stimulated ECM degradation. (oncotarget.com)
Control2
Functions2
  • In addition to transamidation, TG2 also functions as a Gα signaling protein, a protein disulphide isomerase (PDI), a protein kinase and a scaffolding protein. (bvsalud.org)
  • The endoplasmic reticulum (ER) is a network of branching tubules that extends throughout the cytoplasm of the cell and serves multiple functions. (distantreader.org)
Subject1
  • The function of specific proteins from this organism are the subject of intense scientific interest and have been used to derive basic understanding of the functioning similar proteins in higher eukaryotes. (lookformedical.com)
Cells1
  • Cells express a pool of thousands of different proteins that need to be tightly controlled for proper cellular structure, organization, and function. (hindawi.com)
Broad range1
  • In order for a cell to respond to changes in internal and external environmental factors, a broad range of protein co- and post-translational modifications have evolved to expand upon the relatively static properties encoded in protein side-chains. (biologists.com)
Cell2
  • Cytosolic TG2 modifies proteins by the addition of serotonin or other primary amines and in this way affects cell signaling. (bvsalud.org)
  • Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. (lookformedical.com)
Specific1
  • Specific protein-binding measures are often used as assays in diagnostic assessments. (lookformedical.com)
Role1
  • A histone chaperone protein that plays a role in the deposition of NUCLEOSOMES on newly synthesized DNA. (lookformedical.com)
Type1
  • The Sigma-1 receptor is an ER-localized type II membrane protein. (tau.ac.il)