Search results for "Protein Subunit"

showing 10 items of 243 documents

Diversity in AMPA receptor complexes in the brain.

2017

AMPA receptor (AMPAR) complexes comprise four of the AMPAR subunits GluA1-4 and several additional interacting proteins. Subunit composition determines AMPAR function. However, AMPAR function depends to a large extent also on interacting proteins, which influence trafficking to the cell surface, activity-dependent subcellular localization and gating of AMPARs. In this review we report about recent findings on the diversity of AMPAR complexes that allow us to better understand functional properties of native receptors in the brain.

0301 basic medicineProtein subunitCellGatingAMPA receptorBiology03 medical and health sciences0302 clinical medicinemedicineAnimalsHumansReceptors AMPAReceptormusculoskeletal neural and ocular physiologyGeneral NeuroscienceBrainGenetic VariationSubcellular localizationTransport proteinProtein Transport030104 developmental biologymedicine.anatomical_structurenervous systemNeuroscience030217 neurology & neurosurgeryFunction (biology)Current opinion in neurobiology
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Quantitative analysis of the impact of a human pathogenic mutation on the CCT5 chaperonin subunit using a proxy archaeal ortholog

2017

The human chaperonin complex is a ~ 1 MDa nanomachine composed of two octameric rings formed from eight similar but non-identical subunits called CCT. Here, we are elucidating the mechanism of a heritable CCT5 subunit mutation that causes profound neuropathy in humans. In previous work, we introduced an equivalent mutation in an archaeal chaperonin that assembles into two octameric rings like in humans but in which all subunits are identical. We reported that the hexadecamer formed by the mutant subunit is unstable with impaired chaperoning functions. This study quantifies the loss of structural stability in the hexadecamer due to the pathogenic mutation, using differential scanning calorim…

0301 basic medicineProtein subunitMutantBiophysicsHeterologousBiochemistryChaperoninChaperoninlcsh:Biochemistry03 medical and health sciencesDSC differential scanning calorimetryCCT% chaperoninPf Pyrococcus furiosusDenaturation (biochemistry)lcsh:QD415-436Molecular Biologylcsh:QH301-705.5DLS dynamic light scatteringbiologyITC isothermal titration calorimetryWild typeIsothermal titration calorimetryCell BiologyChaperonopathiesbiology.organism_classificationProtein calorimetryNeuropathyPyrococcus furiosus030104 developmental biologyBiochemistryBiophysiclcsh:Biology (General)Pyrococcus furiosusChaperonopathieCCT5; Chaperonin; Chaperonopathies; Neuropathy; Protein calorimetry; Pyrococcus furiosus; Biophysics; Biochemistry; Molecular Biology; Cell BiologyCCT5Pyrococcus furiosuResearch ArticlePf-CD1 Pyrococcus furiosus chaperonin subunit with the last 22 amino acids deletedBiochemistry and Biophysics Reports
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Assembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex

2019

Rotor ATPases are large multisubunit membrane protein complexes found in all kingdoms of life. The membrane parts of these ATPases include a ring-like assembly, so-called c-ring, consisting of several subunits c, plugged by a patch of phospholipids. In this report, we use a nature-inspired approach to model the assembly of the spinach (Spinacia oleracea) c14 ring protein-lipid complex, where partially assembled oligomers are pulled toward each other using a biasing potential. The resulting assemblies contain 23 to 26 encapsulated plug lipids, general position of which corresponds well to experimental maps. However, best fit to experimental data is achieved with 15 to 17 lipids inside the c-…

0301 basic medicineSpinaciaATPaseProtein subunitlipiditBiochemistry Genetics and Molecular Biology (miscellaneous)Biochemistrysolukalvotprotein-lipid interactions03 medical and health sciences0302 clinical medicinecomplex assemblymembrane insertionMolecular Biosciencesmembrane proteinProtein–lipid interactionlcsh:QH301-705.5Molecular BiologyOriginal ResearchbiologyATP synthaseannular lipidsChemistrybiology.organism_classificationadenosiinitrifosfaatti030104 developmental biologyMembranelcsh:Biology (General)Membrane proteinProtein-lipid complex030220 oncology & carcinogenesisbiology.proteinBiophysicslipids (amino acids peptides and proteins)proteiinitFrontiers in Molecular Biosciences
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Membrane insertion and topology of the translocon-associated protein (TRAP) gamma subunit

2017

Translocon-associated protein (TRAP) complex is intimately associated with the ER translocon for the insertion or translocation of newly synthesised proteins in eukaryotic cells. The TRAP complex is comprised of three single-spanning and one multiple-spanning subunits. We have investigated the membrane insertion and topology of the multiple-spanning TRAP-γ subunit by glycosylation mapping and green fluorescent protein fusions both in vitro and in cell cultures. Results demonstrate that TRAP-γ has four transmembrane (TM) segments, an Nt/Ct cytosolic orientation and that the less hydrophobic TM segment inserts efficiently into the membrane only in the cellular context of full-length protein.

0301 basic medicineVesicle-associated membrane protein 8Receptors PeptideProtein subunitBiophysicsReceptors Cytoplasmic and NuclearBiologyEndoplasmic ReticulumTopologyBiochemistryGreen fluorescent protein03 medical and health sciencesN-linked glycosylationMembranes (Biologia)Membrane GlycoproteinsEndoplasmic reticulumCalcium-Binding ProteinsProteïnes de membranaMembrane ProteinsCell BiologyTransloconTransmembrane proteinProtein Subunits030104 developmental biologyHydrophobic and Hydrophilic InteractionsGamma subunit
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Pharmacological disruption of the MID1/α4 interaction reduces mutant Huntingtin levels in primary neuronal cultures.

2017

Expression of mutant Huntingtin (HTT) protein is central to the pathophysiology of Huntington's Disease (HD). The E3 ubiquitin ligase MID1 appears to have a key role in facilitating translation of the mutant HTT mRNA suggesting that interference with the function of this complex could be an attractive therapeutic approach. Here we describe a peptide that is able to disrupt the interaction between MID1 and the α4 protein, a regulatory subunit of protein phosphatase 2A (PP2A). By fusing this peptide to a sequence from the HIV-TAT protein we demonstrate that the peptide can disrupt the interaction within cells and show that this results in a decrease in levels of ribosomal S6 phosphorylation a…

0301 basic medicinecongenital hereditary and neonatal diseases and abnormalitiesHuntingtinMid1 protein mouseProtein subunitUbiquitin-Protein LigasesMutantPrimary Cell CulturePeptide03 medical and health sciencesMiceHuntington's diseasemental disordersmedicineAnimalsHumansHtt protein mouseddc:610Protein Phosphatase 2Neuronschemistry.chemical_classificationMessenger RNAHuntingtin ProteinbiologyChemistryGeneral NeuroscienceProteinsgenetics [Huntingtin Protein]metabolism [Protein Phosphatase 2]metabolism [Proteins]Protein phosphatase 2medicine.diseaseUbiquitin ligaseCell biology030104 developmental biologyHEK293 Cellsmetabolism [Neurons]metabolism [Huntingtin Protein]Mutationbiology.proteinProtein Binding
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alpha 2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth

2017

[EN] COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the endoplasmic reticulum. These vesicles form through the action of the small GTPase ADP-ribosylation factor 1 (ARF1) and the COPI heptameric protein complex (coatomer), which consists of seven subunits (alpha-, beta-, beta' -, gamma-, delta-, epsilon- and xi-COP). In contrast to mammals and yeast, several isoforms for coatomer subunits, with the exception of gamma and delta, have been identified in Arabidopsis. To understand the role of COPI proteins in plant biology, we have identified and characterized a loss-of-function mutant of alpha 2-COP, an Arabidopsis alpha-COP isofo…

0301 basic medicineα2-COPPhysiologyUbiquitin-Protein LigasesProtein subunitMutantSEC31ArabidopsisPlant ScienceEndoplasmic ReticulumCoatomer ProteinP24 family protein03 medical and health sciencessymbols.namesakeBotanyBIOQUIMICA Y BIOLOGIA MOLECULARCOPIICOPIISecretory pathwayCOPICoat proteinArabidopsis ProteinsChemistryEndoplasmic reticulumAlpha 2-COPBiological TransportCOPIGolgi apparatusSEC31.Cell biologyAlpha 1-COPα1-COP030104 developmental biologyCoatomerGolgi apparatussymbolsCOPII Golgi apparatusResearch Paper
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Structural and Functional Characterization of Autophosphorylation in Bacterial Histidine Kinases

2019

Autophosphorylation of histidine kinases (HK) is the first step for signal transduction in bacterial two-component signalling systems. As HKs dimerize, the His residue is phosphorylated in cis or trans depending on whether the ATP molecule used in the reaction is bound to the same or the neighboring subunit, respectively. The cis or trans autophosphorylation results from an alternative directionality in the connection between helices α1 and α2 in the HK DHp domain, in such a way that α2 could be oriented almost 90° counterclockwise or clockwise with respect to α1. Sequence and length variability of this connection appears to lie behind the different directionality and is implicated in partn…

0303 health sciencesKinaseChemistryProtein subunitAutophosphorylation03 medical and health sciencesResponse regulator0302 clinical medicineBiophysicsPhosphorylationDirectionalitySignal transduction030217 neurology & neurosurgeryHistidine030304 developmental biology
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Characterization of crustacyanin-A2 subunit as a component of the organic matrix of gastroliths from the crayfish Cherax quadricarinatus.

2009

AbstractLike the lobsters, some terrestrial crabs and other crayfishes, the Australian red claw crayfish, Cherax quadricarinatus, elaborates in its stomach wall calcium storage structures called gastroliths. For understanding the cyclic elaboration and stabilization of these amorphous calcified structures, we studied the organic matrix (OM) of these paired biomineralizations. After decalcification with acetic acid, we analysed the proteinaceous components of an acetic acid-insoluble fraction by two-dimensional electrophoresis. Nine spots were digested by trpsin and the tryptic peptides were sequenced by nanoLC-nanoESI-MS/MS mass spectrometry. About 100 peptidic sequences were compared to se…

0303 health sciencesMaterials scienceCrustacyanin A2 subunitbiologyProtein subunit030302 biochemistry & molecular biologybiology.organism_classificationCrayfish[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsHomology (biology)[SDV.IB.BIO] Life Sciences [q-bio]/Bioengineering/Biomaterials03 medical and health sciencesAcetic acidchemistry.chemical_compoundchemistryBiochemistryHomarus gammarusCherax quadricarinatusOrganic matrix[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsComputingMilieux_MISCELLANEOUS030304 developmental biology
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Structural and Dynamic Properties of the Homodimeric Hemoglobin from Scapharca inaequivalvis Thr-72→Ile Mutant: Molecular Dynamics Simulation, Low Te…

1998

AbstractMolecular dynamics simulations, low temperature visible absorption spectroscopy, and resonance Raman spectroscopy have been performed on a mutant of the Scapharca inaequivalvis homodimeric hemoglobin, where residue threonine 72, at the subunit interface, has been substituted by isoleucine. Molecular dynamics simulation indicates that in the Thr-72→Ile mutant several residues that have been shown to play a role in ligand binding fluctuate around orientations and distances similar to those observed in the x-ray structure of the CO derivative of the native hemoglobin, although the overall structure remains in the T state. Visible absorption spectroscopy data indicate that in the deoxy …

Absorption spectroscopyProtein subunitDimerResonance Raman spectroscopyMutantBiophysicsHemeSpectrum Analysis Ramanchemistry.chemical_compoundHemoglobinsMutant proteinAnimalsHemeHistidineCarbon MonoxideChemistrySettore BIO/11TemperatureWaterCrystallographyMolluscaSpectrophotometryMutationDimerizationProtein BindingResearch ArticleBiophysical Journal
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Increased protein kinase A regulatory subunit content and cGMP binding in erythrocyte membranes in liver cirrhosis

2003

Abstract Background/Aims : Patients with liver disease show increased plasma cGMP and decreased intracellular cGMP in lymphocytes. The initial aim of this work was to assess whether decreased intracellular cGMP and increased plasma cGMP may be due to increased ATP-dependent release of cGMP from cells. The results obtained led to a new aim: to identify and quantify a protein responsible for the increased cGMP binding found in erythrocyte membranes from patients with liver disease. Methods : ATP-dependent cGMP transport was determined in inside-out vesicles from erythrocyte membranes. cGMP-binding proteins were isolated from the membranes and identified by MALDI-TOF peptide mass fingerprint. …

AdultLiver CirrhosisMalemedicine.medical_specialtyProtein subunitPhosphodiesterase 3Biological Transport ActiveIn Vitro TechniquesBiologyInternal medicinemedicineHumansProtein kinase ACyclic GMPAgedCGMP bindingHepatologyErythrocyte MembraneMiddle AgedCyclic AMP-Dependent Protein KinasesMolecular WeightKineticsProtein SubunitsEndocrinologyCase-Control StudiesSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationCGMP transportbiology.proteinFemaleProtein AcGMP-dependent protein kinaseIntracellularJournal of Hepatology
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