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Protein TransportBiological TransportGolgi ApparatusBiological Transport, ActiveMembrane Transport ProteinsBrefeldin AEndoplasmic ReticulumVesicular Transport ProteinsMembrane ProteinsIntracellular MembranesCarrier ProteinsAxonal TransportCathepsin ATransport VesiclesMolecular Sequence DataCoatomer ProteinAmino Acid SequenceIon TransportSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeVacuolesCell MembraneFungal ProteinsPeasCyclopentanestrans-Golgi NetworkProtein Sorting SignalsKineticsrab2 GTP-Binding ProteinMutationrab GTP-Binding ProteinsCell CompartmentationModels, BiologicalCOP-Coated VesiclesChloroplast ProteinsMonosaccharide Transport ProteinsThylakoidsbeta-FructofuranosidaseRecombinant Fusion ProteinsChloroplastsCoated VesiclesProteinsEndosomesProtein Processing, Post-TranslationalCoat Protein Complex ICell LineElectron TransportEndoplasmic Reticulum, RoughCytoplasmOrganellesrab1 GTP-Binding ProteinsHydrogen-Ion ConcentrationMicroscopy, ElectronProtein BindingADP-Ribosylation FactorsCarboxypeptidasesPlant ProteinsBacterial ProteinsAdenosine TriphosphatasesProtein PrecursorsMembrane GlycoproteinsSodiumNuclear Pore Complex ProteinsAdenosine TriphosphateCloning, MolecularEscherichia coli ProteinsEscherichia coliSequence Homology, Amino AcidGreen Fluorescent ProteinsEndocytosisBase SequenceADP-Ribosylation Factor 1Molecular ChaperonesActive Transport, Cell NucleusTemperatureMasoprocolran GTP-Binding ProteinGenes, FungalMelanotrophsProtein Structure, TertiaryViral Envelope ProteinsGlycosylationCytosolCricetinaeSubcellular FractionsMicrosomesClinical Chemistry TestsCells, CulturedGTP-Binding ProteinsCell NucleusMonensinMicroscopy, FluorescenceAnion Transport ProteinsDogsLuminescent ProteinsCation Transport ProteinsYeastsMicroscopy, ImmunoelectronQa-SNARE ProteinsRecombinant ProteinsDiffusionMicrotubulesN-Ethylmaleimide-Sensitive ProteinsGenetic Complementation TestAdaptor Proteins, Vesicular TransportHeLa CellsGlucoseCell FractionationGlycoside HydrolasesProton-Motive ForceProtein Synthesis InhibitorsSequence AlignmentAmino Acid Transport SystemsGuanine Nucleotide Exchange FactorsCHO CellsGTP PhosphohydrolasesNuclear EnvelopeTime FactorsMitochondriaGuanosine TriphosphateTransfectionModels, MolecularMonomeric GTP-Binding ProteinsChloridesLysosomesProtein ConformationPlasmidsNocodazoleReceptors, PeptideMitochondrial Membrane Transport ProteinsCell-Free SystemAlbuminsSymportersBinding SitesMethylglucosidesAdaptor Protein Complex 1Vesicular stomatitis Indiana virusRNA, MessengerCell PolarityPeptidesArabidopsisPhospholipid Transfer ProteinsSNARE Proteins3-O-MethylglucoseMutagenesis, Site-DirectedOvum TransportATP-Binding Cassette TransportersSignal Recognition ParticleMembrane FusionPlantsMacromolecular SubstancesClathrinDNA, ComplementaryFluorescent Antibody TechniqueAmino Acid Transport Systems, BasicMicrotubule-Associated ProteinsMicroscopy, ConfocalSignal TransductionPotassiumArabidopsis ProteinsNuclear ProteinsDNA PrimersRNA TransportAmino Acid Transport Systems, NeutralBlotting, WesternMethylglycosidesOrganic Cation Transport ProteinsCricetulusProton-Translocating ATPasesTwo-Hybrid System TechniquesGTPase-Activating ProteinsElectrophoresis, Polyacrylamide GelMicroinjectionsLiverPlant LeavesAmino AcidsHeat-Shock ProteinsPhenotypeArginineMolecular WeightGlucose Transport Proteins, FacilitativeExocytosisHSP70 Heat-Shock ProteinsNerve Tissue ProteinsEpithelial CellsAminoisobutyric AcidsMutagenesisDeoxyglucoseCOS CellsProtein BiosynthesisMicrovilliPhotosynthetic Reaction Center Complex ProteinsCell Membrane PermeabilityIntestinal AbsorptionPhloretinGene DeletionHydrolysisTransportationAnionsMembrane Transport ModulatorsGlycoproteins
Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Biological Transport: The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.Golgi Apparatus: A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)Biological Transport, Active: The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.Membrane Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of molecules across a biological membrane. Included in this broad category are proteins involved in active transport (BIOLOGICAL TRANSPORT, ACTIVE), facilitated transport and ION CHANNELS.Brefeldin A: A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Vesicular Transport Proteins: A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Intracellular Membranes: Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Axonal Transport: The directed transport of ORGANELLES and molecules along nerve cell AXONS. Transport can be anterograde (from the cell body) or retrograde (toward the cell body). (Alberts et al., Molecular Biology of the Cell, 3d ed, pG3)Cathepsin A: A carboxypeptidase that catalyzes the release of a C-terminal amino acid with a broad specificity. It also plays a role in the LYSOSOMES by protecting BETA-GALACTOSIDASE and NEURAMINIDASE from degradation. It was formerly classified as EC 3.4.12.1 and EC 3.4.21.13.Transport Vesicles: Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Coatomer Protein: A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Ion Transport: The movement of ions across energy-transducing cell membranes. Transport can be active, passive or facilitated. Ions may travel by themselves (uniport), or as a group of two or more ions in the same (symport) or opposite (antiport) directions.Saccharomyces cerevisiae Proteins: Proteins obtained from the species SACCHAROMYCES CEREVISIAE. 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.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.Fungal Proteins: Proteins found in any species of fungus.Peas: A variable annual leguminous vine (Pisum sativum) that is cultivated for its rounded smooth or wrinkled edible protein-rich seeds, the seed of the pea, and the immature pods with their included seeds. (From Webster's New Collegiate Dictionary, 1973)Cyclopentanes: A group of alicyclic hydrocarbons with the general formula R-C5H9.trans-Golgi Network: A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.Protein Sorting Signals: Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments.Kinetics: The rate dynamics in chemical or physical systems.rab2 GTP-Binding Protein: A protein involved in transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.rab GTP-Binding Proteins: A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.Cell Compartmentation: A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.Models, Biological: Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.COP-Coated Vesicles: TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus.Chloroplast Proteins: Proteins encoded by the CHLOROPLAST GENOME or proteins encoded by the nuclear genome that are imported to and resident in the CHOROPLASTS.Monosaccharide Transport Proteins: A large group of membrane transport proteins that shuttle MONOSACCHARIDES across CELL MEMBRANES.Thylakoids: Membranous cisternae of the CHLOROPLAST containing photosynthetic pigments, reaction centers, and the electron-transport chain. Each thylakoid consists of a flattened sac of membrane enclosing a narrow intra-thylakoid space (Lackie and Dow, Dictionary of Cell Biology, 2nd ed). Individual thylakoids are interconnected and tend to stack to form aggregates called grana. They are found in cyanobacteria and all plants.beta-Fructofuranosidase: A glycoside hydrolase found primarily in PLANTS and YEASTS. It has specificity for beta-D-fructofuranosides such as SUCROSE.Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Chloroplasts: Plant cell inclusion bodies that contain the photosynthetic pigment CHLOROPHYLL, which is associated with the membrane of THYLAKOIDS. Chloroplasts occur in cells of leaves and young stems of plants. They are also found in some forms of PHYTOPLANKTON such as HAPTOPHYTA; DINOFLAGELLATES; DIATOMS; and CRYPTOPHYTA.Coated Vesicles: Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.Proteins: Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.Endosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.Protein Processing, Post-Translational: Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.Coat Protein Complex I: A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Electron Transport: The process by which ELECTRONS are transported from a reduced substrate to molecular OXYGEN. (From Bennington, Saunders Dictionary and Encyclopedia of Laboratory Medicine and Technology, 1984, p270)Endoplasmic Reticulum, Rough: A type of endoplasmic reticulum (ER) where polyribosomes are present on the cytoplasmic surfaces of the ER membranes. This form of ER is prominent in cells specialized for protein secretion and its principal function is to segregate proteins destined for export or intracellular utilization.Cytoplasm: The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)Organelles: Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.rab1 GTP-Binding Proteins: A genetically related subfamily of RAB GTP-BINDING PROTEINS involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS and through early Golgi compartments. This enzyme was formerly listed as EC 3.6.1.47.Hydrogen-Ion Concentration: The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)Microscopy, Electron: Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.ADP-Ribosylation Factors: MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47Carboxypeptidases: Enzymes that act at a free C-terminus of a polypeptide to liberate a single amino acid residue.Plant Proteins: Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.Bacterial Proteins: Proteins found in any species of bacterium.Adenosine Triphosphatases: A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.Protein PrecursorsMembrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Sodium: A member of the alkali group of metals. It has the atomic symbol Na, atomic number 11, and atomic weight 23.Nuclear Pore Complex Proteins: Proteins that form the structure of the NUCLEAR PORE. They are involved in active, facilitated and passive transport of molecules in and out of the CELL NUCLEUS.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Escherichia coli Proteins: Proteins obtained from ESCHERICHIA COLI.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Green Fluorescent Proteins: Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.ADP-Ribosylation Factor 1: ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.Molecular Chaperones: A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.Active Transport, Cell Nucleus: Gated transport mechanisms by which proteins or RNA are moved across the NUCLEAR MEMBRANE.Temperature: The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.Masoprocol: A potent lipoxygenase inhibitor that interferes with arachidonic acid metabolism. The compound also inhibits formyltetrahydrofolate synthetase, carboxylesterase, and cyclooxygenase to a lesser extent. It also serves as an antioxidant in fats and oils.ran GTP-Binding Protein: A monomeric GTP-binding protein involved in nucleocytoplasmic transport of proteins into the nucleus and RNA into the cytoplasm. This enzyme was formerly listed as EC 3.6.1.47.Genes, Fungal: The functional hereditary units of FUNGI.Melanotrophs: Neuroendocrine cells in the INTERMEDIATE LOBE OF PITUITARY. They produce MELANOCYTE STIMULATING HORMONES and other peptides from the post-translational processing of pro-opiomelanocortin (POMC).Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Viral Envelope Proteins: Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.Glycosylation: The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.Cytosol: Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Subcellular Fractions: Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)Microsomes: Artifactual vesicles formed from the endoplasmic reticulum when cells are disrupted. They are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles, and ribosomes. Numerous enzyme activities are associated with the microsomal fraction. (Glick, Glossary of Biochemistry and Molecular Biology, 1990; from Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Clinical Chemistry Tests: Laboratory tests demonstrating the presence of physiologically significant substances in the blood, urine, tissue, and body fluids with application to the diagnosis or therapy of disease.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.GTP-Binding Proteins: Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.Cell Nucleus: Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)Monensin: An antiprotozoal agent produced by Streptomyces cinnamonensis. It exerts its effect during the development of first-generation trophozoites into first-generation schizonts within the intestinal epithelial cells. It does not interfere with hosts' development of acquired immunity to the majority of coccidial species. Monensin is a sodium and proton selective ionophore and is widely used as such in biochemical studies.Microscopy, Fluorescence: Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.Anion Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of negatively charged molecules (anions) across a biological membrane.Dogs: The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)Luminescent Proteins: Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.Cation Transport Proteins: Membrane proteins whose primary function is to facilitate the transport of positively charged molecules (cations) across a biological membrane.Yeasts: A general term for single-celled rounded fungi that reproduce by budding. Brewers' and bakers' yeasts are SACCHAROMYCES CEREVISIAE; therapeutic dried yeast is YEAST, DRIED.Microscopy, Immunoelectron: Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.Qa-SNARE Proteins: A subfamily of Q-SNARE PROTEINS which occupy the same position as syntaxin 1A in the SNARE complex and which also are most similar to syntaxin 1A in their AMINO ACID SEQUENCE. This subfamily is also known as the syntaxins, although a few so called syntaxins are Qc-SNARES.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Diffusion: The tendency of a gas or solute to pass from a point of higher pressure or concentration to a point of lower pressure or concentration and to distribute itself throughout the available space. Diffusion, especially FACILITATED DIFFUSION, is a major mechanism of BIOLOGICAL TRANSPORT.Microtubules: Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS.N-Ethylmaleimide-Sensitive Proteins: ATPases that are members of the AAA protein superfamily (ATPase family Associated with various cellular Activities). The NSFs functions, acting in conjunction with SOLUBLE NSF ATTACHMENT PROTEINS (i.e. SNAPs, which have no relation to SNAP 25), are to dissociate SNARE complexes.Genetic Complementation Test: A test used to determine whether or not complementation (compensation in the form of dominance) will occur in a cell with a given mutant phenotype when another mutant genome, encoding the same mutant phenotype, is introduced into that cell.Adaptor Proteins, Vesicular Transport: A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Glucose: A primary source of energy for living organisms. It is naturally occurring and is found in fruits and other parts of plants in its free state. It is used therapeutically in fluid and nutrient replacement.Cell Fractionation: Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.Glycoside HydrolasesProton-Motive Force: Energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work. Proton-motive force can be generated by a variety of phenomena including the operation of an electron transport chain, illumination of a PURPLE MEMBRANE, and the hydrolysis of ATP by a proton ATPase. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed, p171)Protein Synthesis Inhibitors: Compounds which inhibit the synthesis of proteins. They are usually ANTI-BACTERIAL AGENTS or toxins. Mechanism of the action of inhibition includes the interruption of peptide-chain elongation, the blocking the A site of ribosomes, the misreading of the genetic code or the prevention of the attachment of oligosaccharide side chains to glycoproteins.Sequence Alignment: The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.Amino Acid Transport Systems: Cellular proteins and protein complexes that transport amino acids across biological membranes.Guanine Nucleotide Exchange Factors: Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.GTP Phosphohydrolases: Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.Nuclear Envelope: The membrane system of the CELL NUCLEUS that surrounds the nucleoplasm. It consists of two concentric membranes separated by the perinuclear space. The structures of the envelope where it opens to the cytoplasm are called the nuclear pores (NUCLEAR PORE).Time Factors: Elements of limited time intervals, contributing to particular results or situations.Mitochondria: Semiautonomous, self-reproducing organelles that occur in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. They contain distinctive RIBOSOMES, transfer RNAs (RNA, TRANSFER); AMINO ACYL T RNA SYNTHETASES; and elongation and termination factors. Mitochondria depend upon genes within the nucleus of the cells in which they reside for many essential messenger RNAs (RNA, MESSENGER). Mitochondria are believed to have arisen from aerobic bacteria that established a symbiotic relationship with primitive protoeukaryotes. (King & Stansfield, A Dictionary of Genetics, 4th ed)Guanosine Triphosphate: Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Monomeric GTP-Binding Proteins: A class of monomeric, low molecular weight (20-25 kDa) GTP-binding proteins that regulate a variety of intracellular processes. The GTP bound form of the protein is active and limited by its inherent GTPase activity, which is controlled by an array of GTPase activators, GDP dissociation inhibitors, and guanine nucleotide exchange factors. This enzyme was formerly listed as EC 3.6.1.47Chlorides: Inorganic compounds derived from hydrochloric acid that contain the Cl- ion.Lysosomes: A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.Nocodazole: Nocodazole is an antineoplastic agent which exerts its effect by depolymerizing microtubules.Receptors, Peptide: Cell surface receptors that bind peptide messengers with high affinity and regulate intracellular signals which influence the behavior of cells.Mitochondrial Membrane Transport Proteins: Proteins involved in the transport of specific substances across the membranes of the MITOCHONDRIA.Cell-Free System: A fractionated cell extract that maintains a biological function. A subcellular fraction isolated by ultracentrifugation or other separation techniques must first be isolated so that a process can be studied free from all of the complex side reactions that occur in a cell. The cell-free system is therefore widely used in cell biology. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p166)Albumins: Water-soluble proteins found in egg whites, blood, lymph, and other tissues and fluids. They coagulate upon heating.Symporters: Membrane transporters that co-transport two or more dissimilar molecules in the same direction across a membrane. Usually the transport of one ion or molecule is against its electrochemical gradient and is "powered" by the movement of another ion or molecule with its electrochemical gradient.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.MethylglucosidesAdaptor Protein Complex 1: A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.Vesicular stomatitis Indiana virus: The type species of VESICULOVIRUS causing a disease symptomatically similar to FOOT-AND-MOUTH DISEASE in cattle, horses, and pigs. It may be transmitted to other species including humans, where it causes influenza-like symptoms.RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Cell Polarity: Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Phospholipid Transfer Proteins: A ubiquitous family of proteins that transport PHOSPHOLIPIDS such as PHOSPHATIDYLINOSITOL and PHOSPHATIDYLCHOLINE between membranes. They play an important role in phospholipid metabolism during vesicular transport and SIGNAL TRANSDUCTION.SNARE Proteins: A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.)3-O-Methylglucose: A non-metabolizable glucose analogue that is not phosphorylated by hexokinase. 3-O-Methylglucose is used as a marker to assess glucose transport by evaluating its uptake within various cells and organ systems. (J Neurochem 1993;60(4):1498-504)Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Ovum Transport: Transport of the OVUM or fertilized ovum (ZYGOTE) from the mammalian oviduct (FALLOPIAN TUBES) to the site of EMBRYO IMPLANTATION in the UTERUS.ATP-Binding Cassette Transporters: A family of MEMBRANE TRANSPORT PROTEINS that require ATP hydrolysis for the transport of substrates across membranes. The protein family derives its name from the ATP-binding domain found on the protein.Signal Recognition Particle: A cytosolic ribonucleoprotein complex that acts to induce elongation arrest of nascent presecretory and membrane proteins until the ribosome becomes associated with the rough endoplasmic reticulum. It consists of a 7S RNA and at least six polypeptide subunits (relative molecular masses 9, 14, 19, 54, 68, and 72K).Membrane Fusion: The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes.Plants: Multicellular, eukaryotic life forms of kingdom Plantae (sensu lato), comprising the VIRIDIPLANTAE; RHODOPHYTA; and GLAUCOPHYTA; all of which acquired chloroplasts by direct endosymbiosis of CYANOBACTERIA. They are characterized by a mainly photosynthetic mode of nutrition; essentially unlimited growth at localized regions of cell divisions (MERISTEMS); cellulose within cells providing rigidity; the absence of organs of locomotion; absence of nervous and sensory systems; and an alternation of haploid and diploid generations.Macromolecular Substances: Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.Clathrin: The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Fluorescent Antibody Technique: Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.Amino Acid Transport Systems, Basic: Amino acid transporter systems capable of transporting basic amino acids (AMINO ACIDS, BASIC).Microtubule-Associated Proteins: High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules.Microscopy, Confocal: A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.Signal Transduction: The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.Potassium: An element in the alkali group of metals with an atomic symbol K, atomic number 19, and atomic weight 39.10. It is the chief cation in the intracellular fluid of muscle and other cells. Potassium ion is a strong electrolyte that plays a significant role in the regulation of fluid volume and maintenance of the WATER-ELECTROLYTE BALANCE.Arabidopsis Proteins: Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.Nuclear Proteins: Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.RNA Transport: The process of moving specific RNA molecules from one cellular compartment or region to another by various sorting and transport mechanisms.Amino Acid Transport Systems, Neutral: Amino acid transporter systems capable of transporting neutral amino acids (AMINO ACIDS, NEUTRAL).Blotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.MethylglycosidesOrganic Cation Transport Proteins: A family of proteins involved in the transport of organic cations. They play an important role in the elimination of a variety of endogenous substances, xenobiotics, and their metabolites from the body.Cricetulus: A genus of the family Muridae consisting of eleven species. C. migratorius, the grey or Armenian hamster, and C. griseus, the Chinese hamster, are the two species used in biomedical research.Proton-Translocating ATPases: Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.Two-Hybrid System Techniques: Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.GTPase-Activating Proteins: Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Microinjections: The injection of very small amounts of fluid, often with the aid of a microscope and microsyringes.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Amino Acids: Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins.Heat-Shock Proteins: Proteins which are synthesized in eukaryotic organisms and bacteria in response to hyperthermia and other environmental stresses. They increase thermal tolerance and perform functions essential to cell survival under these conditions.Phenotype: The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.Arginine: An essential amino acid that is physiologically active in the L-form.Molecular Weight: The sum of the weight of all the atoms in a molecule.Glucose Transport Proteins, Facilitative: A family of monosaccharide transport proteins characterized by 12 membrane spanning helices. They facilitate passive diffusion of GLUCOSE across the CELL MEMBRANE.Exocytosis: Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.HSP70 Heat-Shock Proteins: A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.Nerve Tissue ProteinsEpithelial Cells: Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.Aminoisobutyric Acids: A group of compounds that are derivatives of the amino acid 2-amino-2-methylpropanoic acid.Mutagenesis: Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.Deoxyglucose: 2-Deoxy-D-arabino-hexose. An antimetabolite of glucose with antiviral activity.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Protein Biosynthesis: The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS.Microvilli: Minute projections of cell membranes which greatly increase the surface area of the cell.Photosynthetic Reaction Center Complex Proteins: Protein complexes that take part in the process of PHOTOSYNTHESIS. They are located within the THYLAKOID MEMBRANES of plant CHLOROPLASTS and a variety of structures in more primitive organisms. There are two major complexes involved in the photosynthetic process called PHOTOSYSTEM I and PHOTOSYSTEM II.Cell Membrane Permeability: A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.Intestinal Absorption: Uptake of substances through the lining of the INTESTINES.PhloretinGene Deletion: A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.Hydrolysis: The process of cleaving a chemical compound by the addition of a molecule of water.Transportation: The means of moving persons, animals, goods, or materials from one place to another.Anions: Negatively charged atoms, radicals or groups of atoms which travel to the anode or positive pole during electrolysis.Membrane Transport Modulators: Agents that affect ION PUMPS; ION CHANNELS; ABC TRANSPORTERS; and other MEMBRANE TRANSPORT PROTEINS.Glycoproteins: Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.

A novel in vivo assay for the analysis of protein-protein interaction. (1/21932)

The Ras Recruitment System (RRS) is a method for identification and isolation of protein-protein interaction. The method is based on translocation of cytoplasmic mammalian Ras protein to the inner leaflet of the plasma membrane through protein-protein interaction. The system is studied in a temperature-sensitive yeast strain where the yeast Ras guanyl nucleotide exchange factor is inactive at 36 degrees C. Protein-protein interaction results in cell growth at the restrictive temperature. We developed a gene reporter assay for the analysis of protein-protein interaction in mammalian cells. Ras activation in mammalian cells induces the mitogen-activated kinase cascade (MAPK), which can be monitored using Ras-dependent reporter genes. This greatly extends the usefulness of the system and provides a novel assay for protein-protein interaction in mammalian cells.  (+info)

Decisive structural determinants for the interaction of proline derivatives with the intestinal H+/peptide symporter. (2/21932)

To elucidate the decisive structural factors relevant for dipeptide-carrier interaction, the affinity of short amide and imide derivatives for the intestinal H+/peptide symporter (PEPT1) was investigated by measuring their ability to inhibit Gly-Sar transport in Caco-2 cells. Dipeptides with proline or alanine in the C-terminal position displayed affinity constants (Ki) of 0.15-1.2 mM and 0.08-9.5 mM, respectively. There was no clear relationship between hydrophobicity, size or ionization status of the N-terminal amino acid and the affinity of the dipeptides. However, analyzing the individual peptide bond conformations of Xaa-Pro dipeptides, a striking correlation between the cis/trans ratios (trans contents 24-70%) and the affinity constants was observed. After correcting the Ki values for the incompetent cis isomers, the Ki corr values of most dipeptides were in a small range of 0.1-0.16 mM. This result revealed the decisive role of peptide bond conformation even for a transport protein that is quite promiscuous in substrate translocation. When measuring affinity constants of Xaa-Pro and Xaa-Sar dipeptides, the cis/trans ratios cannot be ignored. Lower affinities of Lys-Pro, Arg-Pro and Pro-Pro indicate that additional molecular factors affect their binding at PEPT1. The Ki values obtained for the corresponding Xaa-Ala dipeptides support this conclusion. Potential substrates or inhibitors of peptide transport were found among Xaa-piperidides and Xaa-thiazolidides. Dipeptides with N-terminal proline displayed a very diverse affinity profile. However, in contrast to current knowledge, several Pro-Xaa dipeptides such as Pro-Leu, Pro-Tyr and Pro-Pro are recognized by PEPT1 with appreciable affinities. Binding seems mainly determined by the hydrophobicity of the C-terminal amino acid and the rigidity of the structure.  (+info)

Involvement of proline-rich tyrosine kinase 2 in platelet activation: tyrosine phosphorylation mostly dependent on alphaIIbbeta3 integrin and protein kinase C, translocation to the cytoskeleton and association with Shc through Grb2. (3/21932)

Proline-rich tyrosine kinase 2 (Pyk2) (also known as RAFTK, CAKbeta or CADTK) has been identified as a member of the focal adhesion kinase (FAK) family of protein-tyrosine kinases and it has been suggested that the mode of Pyk2 activation is distinct from that of FAK. In the present study we investigated the mode of Pyk2 activation in human platelets. When platelets were stimulated with thrombin, Pyk2, as well as FAK, was markedly tyrosine-phosphorylated, in a manner mostly dependent on alphaIIbbeta3 integrin-mediated aggregation. The residual Pyk2 tyrosine phosphorylation observed in the absence of platelet aggregation was completely abolished by pretreatment with BAPTA/AM [bis-(o-aminophenoxy)ethane-N,N,N',N'-tetra-acetic acid acetoxymethyl ester]. The Pyk2 phosphorylation was inhibited by protein kinase C (PKC) inhibitors at concentrations that inhibited platelet aggregation. In contrast, direct activation of PKC with the active phorbol ester PMA induced the tyrosine phosphorylation of Pyk2 and FAK but only when platelets were fully aggregated with the exogenous addition of fibrinogen (the ligand for alphaIIbbeta3 integrin). Furthermore, PMA-induced Pyk2 (and FAK) tyrosine phosphorylation was also observed when platelets adhered to immobilized fibrinogen. The activation of the von Willebrand factor (vWF)--glycoprotein Ib pathway with botrocetin together with vWF failed to induce Pyk2 (and FAK) tyrosine phosphorylation. Most Pyk2 and FAK was present in the cytosol and membrane skeleton fractions in unstimulated platelets. When platelets were stimulated with thrombin, both Pyk2 and FAK were translocated to the cytoskeleton in an aggregation-dependent manner. In immunoprecipitation studies, Pyk2, as well as FAK, seemed to associate with Shc through Grb2. With the use of glutathione S-transferase fusion proteins containing Shc-SH2, Grb2-SH2, and Grb2 N-terminal and C-terminal SH3 domains, it was implied that the proline-rich region of Pyk2 (and FAK) binds to the N-terminal SH3 domain of Grb2 and that the phosphotyrosine residue of Shc binds to the SH2 domain of Grb2. Although Pyk2 and FAK have been reported to be differentially regulated in many cell types, our results suggest that, in human platelets, the mode of Pyk2 activation is mostly similar to that of FAK, in terms of alphaIIbbeta3 integrin-dependent and PKC-dependent tyrosine phosphorylation. Furthermore, Pyk2, as well as FAK, might have one or more important roles in post-aggregation tyrosine phosphorylation events, in association with the cytoskeleton and through interaction with adapter proteins including Grb2 and Shc.  (+info)

Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. (4/21932)

Aut7p, a protein recently implicated in autophagic events in the yeast Saccharomyces cerevisiae, exhibits significant homology to a mammalian protein, p16, herein termed GATE-16 (Golgi-associated ATPase Enhancer of 16 kDa), a novel intra-Golgi transport factor. Here we provide evidence for the involvement of Aut7p in different membrane trafficking processes. Aut7p largely substitutes for the activity of GATE-16 in mammalian intra-Golgi transport in vitro. In vivo, AUT7 interacts genetically with endoplasmic reticulum to Golgi SNAREs, specifically with BET1 and SEC22. Aut7p interacts physically with the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum to Golgi vesicular transport, and Nyv1p, implicated in vacuolar inheritance. We suggest that, in addition to its role in autophagocytosis, Aut7p has pleiotropic effects and participates in at least two membrane traffic events.  (+info)

Targeting motifs and functional parameters governing the assembly of connexins into gap junctions. (5/21932)

To study the assembly of gap junctions, connexin--green-fluorescent-protein (Cx--GFP) chimeras were expressed in COS-7 and HeLa cells. Cx26-- and Cx32--GFP were targeted to gap junctions where they formed functional channels that transferred Lucifer Yellow. A series of Cx32--GFP chimeras, truncated from the C-terminal cytoplasmic tail, were studied to identify amino acid sequences governing targeting from intracellular assembly sites to the gap junction. Extensive truncation of Cx32 resulted in failure to integrate into membranes. Truncation of Cx32 to residue 207, corresponding to removal of most of the 78 amino acids on the cytoplasmic C-terminal tail, led to arrest in the endoplasmic reticulum and incomplete oligomerization. However, truncation to amino acid 219 did not impair Cx oligomerization and connexon hemichannels were targeted to the plasma membrane. It was concluded that a crucial gap-junction targeting sequence resides between amino acid residues 207 and 219 on the cytoplasmic C-terminal tail of Cx32. Studies of a Cx32E208K mutation identified this as one of the key amino acids dictating targeting to the gap junction, although oligomerization of this site-specific mutation into hexameric hemichannels was relatively unimpaired. The studies show that expression of these Cx--GFP constructs in mammalian cells allowed an analysis of amino acid residues involved in gap-junction assembly.  (+info)

Identification of mammalian TOM22 as a subunit of the preprotein translocase of the mitochondrial outer membrane. (6/21932)

A mitochondrial outer membrane protein of approximately 22 kDa (1C9-2) was purified from Vero cells assessing immunoreactivity with a monoclonal antibody, and the cDNA was cloned based on the partial amino acid sequence of the trypsin-digested fragments. 1C9-2 had 19-20% sequence identity to fungal Tom22, a component of the preprotein translocase of the outer membrane (the TOM complex) with receptor and organizer functions. Despite such a low sequence identity, both shared a remarkable structural similarity in the hydrophobicity profile, membrane topology in the Ncyt-Cin orientation through a transmembrane domain in the middle of the molecule, and the abundant acidic amino acid residues in the N-terminal domain. The antibodies against 1C9-2 inhibited the import of a matrix-targeted preprotein into isolated mitochondria. Blue native polyacrylamide gel electrophoresis of digitonin-solubilized outer membranes revealed that 1C9-2 is firmly associated with TOM40 in the approximately 400-kDa complex, with a size and composition similar to those of the fungal TOM core complex. Furthermore, 1C9-2 complemented the defects of growth and mitochondrial protein import in Deltatom22 yeast cells. Taken together, these results demonstrate that 1C9-2 is a functional homologue of fungal Tom22 and functions as a component of the TOM complex.  (+info)

Inhibition of NFkappaB by methyl chlorogenate from Eriobotrya japonica. (7/21932)

Methylchlorogenic acid (MC) is one of the main components in the leaves of Eriobotrya japonica. We previously reported that MC is the most potent antioxidant among several components of Eriobotrya japonica, and its antioxidant activity is stronger than that of chlorogenic acid. Antioxidants are expected to inhibit redox-sensitive NFkappaB activation since NFkappaB is readily influenced by cellular oxidative state. Based on these findings, in vivo experiments with MC were conducted to determine its ability to downregulate the NFkappaB activation in mouse liver. Results clearly showed that MC is a potent suppressor of BHP-induced NFkappaB activation. We observed a significant reduction by MC on BHP-induced translocation of p65 subunit of NFkappaB. This may be due to formation of p50/p65 heterodimer, which is mainly inducible NFkappaB. MC slightly blocked the BHP-induced IkappaB alpha degradation. There is a possibility of IkappaB alpha resynthesis via activated NFkappaB during a 5 h waiting period following BHP injection. The present results suggest that MC may inhibit NFkappaB activation, exhibiting its ability to downregulate the NFkappaB-dependent gene expression. Thus, it can be expected that MC may have potential for therapeutic intervention on various NFkappaB-dependent pathological conditions such as inflammatory or possibly mutagenic processes.  (+info)

Functional and structural characterization of synthetic HIV-1 Vpr that transduces cells, localizes to the nucleus, and induces G2 cell cycle arrest. (8/21932)

Human immunodeficiency virus (HIV) Vpr contributes to nuclear import of the viral pre-integration complex and induces G(2) cell cycle arrest. We describe the production of synthetic Vpr that permitted the first studies on the structure and folding of the full-length protein. Vpr is unstructured at neutral pH, whereas under acidic conditions or upon addition of trifluorethanol it adopts alpha-helical structures. Vpr forms dimers in aqueous trifluorethanol, whereas oligomers exist in pure water. (1)H NMR spectroscopy allows the signal assignment of N- and C-terminal amino acid residues; however, the central section of the molecule is obscured by self-association. These findings suggest that the in vivo folding of Vpr may require structure-stabilizing interacting factors such as previously described interacting cellular and viral proteins or nucleic acids. In biological studies we found that Vpr is efficiently taken up from the extracellular medium by cells in a process that occurs independent of other HIV-1 proteins and appears to be independent of cellular receptors. Following cellular uptake, Vpr is efficiently imported into the nucleus of transduced cells. Extracellular addition of Vpr induces G(2) cell cycle arrest in dividing cells. Together, these findings raise the possibility that circulating forms of Vpr observed in HIV-infected patients may exert biological effects on a broad range of host target cells.  (+info)

HEK AR Nuclear Translocation Assay Kit Kit-1653 - Creative BioMartHEK AR Nuclear Translocation Assay Kit Kit-1653 - Creative BioMart
Purified HEK AR Nuclear Translocation Assay Kit from Creative Biomart. HEK AR Nuclear Translocation Assay Kit can be used for research.
bis 104 pq 29 ans ss i 2009 - Increased numbers of GLUT-4 receptors transport glucose from blood into the ell where it is...bis 104 pq 29 ans ss i 2009 - Increased numbers of GLUT-4 receptors transport glucose from blood into the ell where it is...
View Notes - bis_104_pq_29_ans_ss_i_2009 from BIS BIS 104 at UC Davis. Increased numbers of GLUT-4 receptors transport glucose from blood into the ell where it is rapidly phosphorylated to maintain
Parkinsons disease : Alpha synucleins non-amyloidal component (NAC) aids the proteins movement through axons - https:/...Parkinson's disease : Alpha synuclein's non-amyloidal component (NAC) aids the protein's movement through axons - https:/...
Parkinsons disease : Alpha synucleins non-amyloidal component (NAC) aids the proteins movement through axons - Featured https://debuglies.com
AMRENDRA KUMAR AJAYAMRENDRA KUMAR AJAY
Insulin-stimulated translocation of glucose transporter 4 (GLUT4) to cell membrane leading to glucose uptake is the rate-limiting step in diabetes. It is also a defined target of antidiabetic drug research. Existing GLUT4 translocation assays are based on time-consuming immunoassays and are hampered by assay variability and low sensitivity. We describe a real-time, visual, cell-based qualitative GLUT4 translocation assay using CHO-HIRc-myc-GLUT4eGFP cells that stably express myc- and eGFP-tagged GLUT4 in addition to human insulin receptor (HIRc). GLUT4 translocation is visualized by live cell imaging based on GFP fluorescence by employing a cooled charge-coupled device camera attached to a fluorescent microscope. This video imaging method and further quantitative analysis of GLUT4 on the cell membrane provide rapid and foolproof visual evidence that this method is suitable for screening GLUT4 translocation modulators.. ...
GO:0032600 - wiki-painGO:0032600 - wiki-pain
The table below shows the top 100 pain related interactions that have been reported for chemokine receptor transport out of membrane raft. They are ordered first by their pain relevance and then by number of times they were reported for chemokine receptor transport out of membrane raft. Please click on the INT link to display more detailed information on each interaction. ...
TAxI Shuttles Protein Cargo into Spinal CordTAxI Shuttles Protein Cargo into Spinal Cord
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Gentaur Molecular :Cusabio \ Human Protein transport protein Sec24A(SEC24A) ELISA kit SpeciesHuman \ CSB-EL020950HUGentaur Molecular :Cusabio \ Human Protein transport protein Sec24A(SEC24A) ELISA kit SpeciesHuman \ CSB-EL020950HU
Gentaur molecular products has all kinds of products like :search , Cusabio \ Human Protein transport protein Sec24A(SEC24A) ELISA kit SpeciesHuman \ CSB-EL020950HU for more molecular products just contact us
Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope...Stable association of chloroplastic precursors with protein translocation complexes that contain proteins from both envelope...
Recent identification of several members of the chloroplastic protein translocation machinery has allowed for further refinement of our understanding of the mechanism by which precursors are transported into chloroplasts. We have attempted to define the composition of complexes that form during translocation using co‐immunoprecipitation techniques with antibodies specific to translocation components. We have observed that precursors could be found in stable association with translocation complexes after solubilization with a mild detergent, decylmaltoside. Characterization of these complexes has led to two conclusions: (i) that under limiting ATP conditions, precursors associated with translocation complexes containing components of the outer and inner envelope membranes; and (ii) that the chaperone ClpC, a stromal Hsp100 homolog, was associated with precursor‐containing complexes under these limiting ATP conditions.. The data presented here suggest a new role for the stromal Hsp100 homolog ...
wingfield.npb101.readings.2009 - adhesion molecules gap junctions receptors transport molecules Feedback loops(negative and...wingfield.npb101.readings.2009 - adhesion molecules gap junctions receptors transport molecules Feedback loops(negative and...
View Notes - wingfield.npb101.readings.2009 from NPB NPB 101 at UC Davis. adhesion molecules, gap junctions, receptors, transport molecules Feedback loops (negative and positive) How are chemical
KEGG PATHWAY: Protein exportKEGG PATHWAY: Protein export
The protein export is the active transport of proteins from the cytoplasm to the exterior of the cell, or to the periplasmic compartment in Gram-negative bacteria. The sec dependent pathway is the general protein export system that transports newly synthesized proteins into or across the cell membrane. The translocation channel is formed from a conserved trimeric membrane protein complex, called the Sec61/SecY complex. The twin-arginine translocation (Tat) pathway is another protein transport system that transports folded proteins in bacteria, archaea, and chloroplasts. Many Tat systems comprise three functionally different membrane proteins, TatA, TatB, and TatC, but TatA and TatE seem to have overlapping functions, with TatA having by far the more important role ...
Subcellular localization determines the availability of non-targeted proteins to plasmodesmatal transportSubcellular localization determines the availability of non-targeted proteins to plasmodesmatal transport
A significant population of leaf cells contain plasmodesmata in a dilated state, allowing macromolecular transport between cells. Protein movement potential is regulated by subcellular address and size. These parameters of protein movement illustrate how gradients of signaling macromolecules could b …
US Patent # 9,595,017. Asset tracking and monitoring along a transport route - Patents.comUS Patent # 9,595,017. Asset tracking and monitoring along a transport route - Patents.com
A system and computer program product for tracking and monitoring assets along a transport route. The system includes at least one receiver for receiving asset identifications transmitted from the as
Detecting intracellular translocation of native proteins quantitatively at the single cell level - Chemical Science (RSC...Detecting intracellular translocation of native proteins quantitatively at the single cell level - Chemical Science (RSC...
The intracellular localization and movement (i.e. translocation) of proteins are critically correlated with the functions and activation states of these proteins. Simple and accessible detection methods that can rapidly screen a large cell population with single cell resolution have been seriously lacking. I
Mitochondrial Metabolite Channel Functions in Protein TransportMitochondrial Metabolite Channel Functions in Protein Transport
The research labs of the associate professor Dr. Thomas Becker and Prof. Dr. Nikolaus Pfanner from the Institute for Biochemistry and Molecular Biology at the University of Freiburg discovered a function of the metabolite channel of the mitochondrial outer membrane in protein transport.
Some Effects of Ionizing Radiation on Translocation in Plants | ScienceSome Effects of Ionizing Radiation on Translocation in Plants | Science
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Re: %files section of SPEC fileRe: %files section of SPEC file
buildroot}/etc/ ...and placed in the final destination of: /etc I keep getting the entire %{buildroot} created on the destination host. TIA ...
1 - Agea forex online1 - Agea forex online
Put call options forex cargo #### AGEA FOREX ONLINE Tabella correlazione forex charts #### Forex trading strategies with bollinger bands
Intracellular translocation of the decapeptide carboxyl terminal of G(i)3 alpha induces the dual phosphorylation of p42/p44 MAP...Intracellular translocation of the decapeptide carboxyl terminal of G(i)3 alpha induces the dual phosphorylation of p42/p44 MAP...
The carboxyl terminal of heterotrimeric G protein alpha subunits binds both G protein-coupled receptors and mastoparan (MP), a tetradecapeptide allostere. Moreover, peptides corresponding to the carboxyl domains of G(i)3 alpha and G(t) display intrinsic biological activities in cell-free systems. Thus, the purpose of this study was to develop a cell penetrant delivery system to further investigate the biological properties of a peptide mimetic of the G(i)3 alpha carboxyl terminal (G(i)3 alpha(346-355); H-KNNLKECGLY-NH2). Kinetic studies, using a CFDA-conjugated analogue of G(i)3 alpha(346-355), confirmed the rapid and efficient intracellular translocation of TP10-G(i)3 alpha(346-355) (t(0.5) = 3 min). Translocated G(i)3 alpha(346-355), but not other bioactive cargoes derived from PKC and the CB1 cannabinoid receptor, promoted the dual phosphorylation of p42/p44 MAPK without adverse changes in cellular viability. The relative specificity of this novel biological activity was further confirmed by ...
Plus itPlus it
Several lines of evidence indicated that CIA5 is an essential translocon component for protein import into chloroplasts. Null cia5 mutants were lethal and accumulated unprocessed chloroplast precursor proteins. Chloroplasts from cia5 mutants were specifically defective in protein translocation across the inner membrane. CIA5 was specifically copurified with other major translocon components, and cia5 mutant chloroplasts had reduced levels of other translocon components. Furthermore, the expression level of CIA5 is comparable to other major translocon components. Because CIA5 is located in the inner membrane, it should be called a Tic protein. On SDS-PAGE, pea CIA5 migrated in between pea Tic20 and Tic22, very close to Tic22 (data not shown). We have therefore renamed CIA5 as Arabidopsis Tic21 (At Tic21).. CIA5/At Tic21 is deeply embedded in the inner membrane, and its cyanobacterial homologues have some similarities to proteins that are annotated as amino acid transporters and sugar permeases. ...
Protein Movement Across Membranes PDF - Free books downloadProtein Movement Across Membranes PDF - Free books download
This book addresses the most recent advances in the transport of proteins across a variety of biological membranes. In addressing this topic, this volume includes several new twists not previously addressed in the literature. In the last few years, the study of protein translocation has been revolutionized by the availability of structural information on many of the components and complexes involved in the process. Unlike earlier books written on protein translocation, this volume considers these advances. In addition, several chapters discuss facets of protein translocation from a systems biology perspective, considered by many to be the next paradigm for biological study. Readers of this book will come away with a deeper understanding of the problems facing researchers of protein translocation and see how the most modern biological techniques and approaches are being recruited to answer those questions. The chapters are also written such that problems awaiting future investigation are clearly ...
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Trafficking of postsynaptic receptors is a means of regulating synaptic function in the dendrites, yet the details of delivery processes are not well explored. In this study, we present two general pathways for receptor transport to synaptic sites in the dendrite. Six of the seven GPCRs examined notably preferred passive diffusion from the cell body to the dendrite branches. This energy efficient transport via the plasma membrane is likely shared by most postsynaptic GPCRs. An alternate pathway, as seen with 5-HT1B, retains receptors in transport vesicles. At the cost of expending energy on active transport, 5-HT1B is maintained as a readily accessible source of mobile receptors for rapid exocytotic recruitment to the membrane throughout the dendrites. Though unique among the receptors included in our study, this active trafficking pathway may be used by yet unexamined receptors.. Previous postsynaptic GPCR studies describing intracellular trafficking are mostly limited to receptor recycling or ...
Like a Microscopic Mars Rover, a New Technique Tracks Individual Protein Movement on Live CellsLike a Microscopic Mars Rover, a New Technique Tracks Individual Protein Movement on Live Cells
The piece of gold that Richard Taylor was thrilled to track down weighed less than a single bacterium. Taylor, a postdoctoral fellow at the Max Planck Institute, was working to follow individual nanogold-labeled molecules that move just nanometers, billionths of a meter.
SEC61 (YLR378C) Result Summary | BioGRIDSEC61 (YLR378C) Result Summary | BioGRID
Conserved ER Protein Translocation Channel; Essential Subunit Of Sec61 Complex (Sec61p, Sbh1p, And Sss1p); Forms Channel For SRP-dependent Protein Import; With Sec63 Complex Allows SRP-independent Protein Import Into ER; Involved In Posttranslational Soluble Protein Import Into The ER, ERAD Of Soluble Substrates, And Misfolded Soluble Protein Export From The ER
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Degradation of the plant hormone cytokinin is controlled by cytokinin oxidase/dehydrogenase (CKX) enzymes. The molecular and cellular behavior of these proteins is still largely unknown. In this study, we show that CKX1 is a type-II single-pass membrane protein that predominantly localizes to the endoplasmic reticulum (ER). This indicates that this CKX isoform is a bona fide ER protein directly controlling the cytokinin which triggers the signaling from the ER. By using various approaches, we demonstrate that CKX1 forms homodimers and homooligomers in vivo. The N-terminal part of CKX1 was necessary and sufficient for the protein oligomerization as well as for targeting and retention in the ER. Moreover, we show that protein-protein interaction is largely facilitated by transmembrane helices and depends on a functional GxxxG-like interaction motif. Importantly, mutations rendering CKX1 monomeric interfere with its steady-state localization in the ER and cause a loss of the CKX1 biological ...
Mapping the insulin/GLUT4 circuitry | Garvan Institute of Medical ResearchMapping the insulin/GLUT4 circuitry | Garvan Institute of Medical Research
One of the most important metabolic actions of insulin is catalysing glucose uptake into skeletal muscle and adipose tissue. This is accomplished via activation of the PI3K/Akt signalling pathway and subsequent translocation of GLUT4 from intracellular storage vesicles to the plasma membrane. As such, this represents an ideal system for studying the convergence of signal transduction and protein trafficking. The GLUT4 translocation process is complex, but can be dissected into at least 4 discrete trafficking steps. This raises the question as to which of these is the major regulated step in insulin-stimulated GLUT4 translocation. Numerous molecules have been reported to regulate GLUT4 trafficking. However, with the exception of TBC1D4, the molecular details of these distal signalling arms of the insulin signalling network and how they modify distinct steps of GLUT4 trafficking have not been established. We discuss the need to adopt a more global approach to expand and deepen our understanding of the
Membrane-protein insertion: One helix and one amino acid at a time | School of PhysicsMembrane-protein insertion: One helix and one amino acid at a time | School of Physics
Membrane proteins are critical components of all cells, controlling, e.g., signaling, nutrient exchange, and energy production, and are the target of over half of all drugs currently in production. At an early stage of their synthesis, nearly all membrane proteins are directed to a protein-conducting channel, the SecY/Sec61 complex, which permits access to the membrane via its lateral gate.
High ContentHigh Content
There are two automated imaging systems in the Facility that can be used for HCS applications. The first is an InCell 6000 which is a semi-confocal imaging system designed to image cells cultured in standard format multi-well plates (although it can also image cells on slides). In addition to imaging fixed cells, the system has many features which make it suitable for live cell analysis including temperature control, CO2 regulation and liquid handling. The InCell 6000 is equipped with a Caliper Twister II robotic plate loader which significantly increases the throughput capability of the system. Potential applications for this system include live/dead analysis, cell cycle analysis, apoptosis, cytoplasmic/ nucleus translocation assays, DNA damage, tube formation (angiogenesis), neurite outgrowth, micronucleus assays, morphometric analysis (tubulin) and cell migration ...
Introduction: Regulatory processes, an emerging feature in intracellular membrane traffic<...Introduction: Regulatory processes, an emerging feature in intracellular membrane traffic<...
TY - CHAP. T1 - Introduction: Regulatory processes, an emerging feature in intracellular membrane traffic. AU - Keränen, Sirkka. AU - Jäntti, Jussi. PY - 2004. Y1 - 2004. N2 - The subject of this volume is the molecular mechanism of the intracellular membrane trafficking, a central eukaryotic cell biological process. In the post genomic era, essential molecules involved in intracellular membrane/protein transport are emerging with increasing pace. The present challenge is to compile the molecular networks that govern these processes. Understanding of regulatory processes and participating molecules are likely to reveal global cellular regulatory circuits that couple membrane trafficking with other cellular functions. The part of the membrane transport machinery, which forms stabile protein complexes is rather well known already. However, the regulatory mechanisms that link these more stabile complexes to other cellular functions are only starting to emerge. This book focuses on the regulatory ...
Organelle Biogenesis and Positioning in Plants | Biochemical Society TransactionsOrganelle Biogenesis and Positioning in Plants | Biochemical Society Transactions
The biogenesis and positioning of organelles involves complex interacting processes and precise control. Progress in our understanding is being made rapidly as advances in analysing the nuclear and organellar genome and proteome combine with developments in live-cell microscopy and manipulation at the subcellular level. This paper introduces the collected papers resulting from Organelle Biogenesis and Positioning in Plants, the 2009 Biochemical Society Annual Symposium. Including papers on the nuclear envelope and all major organelles, it considers current knowledge and progress towards unifying themes that will elucidate the mechanisms by which cells generate the correct complement of organelles and adapt and change it in response to environmental and developmental signals.. ...
2018 Protein Transport Across Cell Membranes Conference GRC2018 Protein Transport Across Cell Membranes Conference GRC
The 2018 Gordon Research Conference on Protein Transport Across Cell Membranes will be held in Galveston, TX. Apply today to reserve your spot.
The complete exosome workflow solution: from isolation to characterization of RNA cargo | Exosome RNAThe complete exosome workflow solution: from isolation to characterization of RNA cargo | Exosome RNA
Exosomes are small (30-150 nm) vesicles containing unique RNA and protein cargo, secreted by all cell types in culture. They are also found in abundance in body fluids including blood, saliva, and urine. At the moment, the mechanism of exosome formation, the makeup of the cargo, biological pathways, and resulting
Inhibition of Delta pH pathway protein transport by ant | Open-iInhibition of Delta pH pathway protein transport by ant | Open-i
Inhibition of Delta pH pathway protein transport by antibodies to Hcf106. (A) Maize thylakoids were preincubated with 0.1 mg/ml anti-Hcf106 or preimmune (PI) Ig
Diamond Publications - Search ResultsDiamond Publications - Search Results
Abstract: The β-barrel assembly machinery (BAM) inserts outer membrane β-barrel proteins (OMPs) in the outer membrane of Gram-negative bacteria. In Enterobacteriacea, BAM also mediates export of the stress sensor lipoprotein RcsF to the cell surface by assembling RcsF-OMP complexes. Here, we report the crystal structure of the key BAM component BamA in complex with RcsF. BamA adopts an inward-open conformation, with the lateral gate to the membrane closed. RcsF is lodged deep within the lumen of the BamA barrel, binding regions proposed to undergo outward and lateral opening during OMP insertion. On the basis of our structural and biochemical data, we propose a push-and-pull model for RcsF export following conformational cycling of BamA, and provide a mechanistic explanation for how RcsF uses its interaction with BamA to detect envelope stress. Our data also suggest that the flux of incoming OMP substrates is involved in the control of BAM activity ...
The Brain and the Mind, page 1The Brain and the Mind, page 1
Yet there are arguments made against this view. Although memory has never been found - and may never be found - in the human brain, there are attempts nevertheless to explain it as such; a particular experience for example can be physically monitored; the neuronal movements can be mapped, which will imply a technology that can see INTO neurons and all the protein movements occurring therein. Since this will involve millions of processes within a single neuron, well need an impressive supercomputer to do all this. But lets say we do all, and discover that "this" cluster of neurons corresponds to this memory; and show it that everytime this memory is activated, these proteins are assembled just like that. It seems almost absurd in the complexity; and even logically, we know that correlation isnt causation, and that is the real kicker about science and mind. You cant ever prove or unprove it. It just is: it stays as it is and we live as we live, and in the end, we die, and we dissolve into the ...
Anti-EEA1 抗体 [1G11] - Early Endosome Marker (ab70521)Anti-EEA1 抗体 [1G11] - Early Endosome Marker (ab70521)
マウス・モノクローナル抗体 ab70521 交差種: Hu 適用: ICC/IF…EEA1抗体一覧…画像、プロトコール、文献などWeb上の情報が満載のアブカムの Antibody 製品。国内在庫と品質保証制度も充実。
Cargo NewsCargo News
Cargo | Official Trailer [HD] | Netflix, Cargo | Finalist of Tropfest Australia 2013, Cargo - Daca ploaia s-ar opri (Official Video), Cargo - Ziua Vrajitoarelor (Ziua Vrajitoarelor, 1998), Cargo - Nu ma lasa sa-mi fie dor (Official Video)
Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine...Endosomal localization and receptor dynamics determine tyrosine phosphorylation of hepatocyte growth factor-regulated tyrosine...
Hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) is a prominent substrate for activated tyrosine kinase receptors that has been proposed to play a role in endosomal membrane trafficking. The protein contains a FYVE domain, which specifically binds to the lipid phosphatidylinositol (PI) 3-phosphate (PI 3-P). We show that this interaction is required both for correct localization of the protein to endosomes that only partially coincides with early endosomal autoantigen 1 and for efficient tyrosine phosphorylation of the protein in response to epidermal growth factor stimulation. Treatment with wortmannin reveals that Hrs phosphorylation also requires PI 3-kinase activity, which is necessary to generate the PI 3-P required for localization. We have used both hypertonic media and expression of a dominant-negative form of dynamin (K44A) to inhibit endocytosis; under which conditions, receptor stimulation fails to elicit phosphorylation of Hrs. Our results provide a clear example of the
RCSB PDB - Protein Feature View - Hepatocyte growth factor-regulated tyrosine kinase substrate - Q960X8 (HRS DROME)RCSB PDB - Protein Feature View - Hepatocyte growth factor-regulated tyrosine kinase substrate - Q960X8 (HRS DROME)
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Protein targeting by the bacterial twin-arginine translocation (Tat) pathway. - Oxford NeuroscienceProtein targeting by the bacterial twin-arginine translocation (Tat) pathway. - Oxford Neuroscience
The Tat (twin-arginine translocation) protein export system is found in the cytoplasmic membrane of most prokaryotes and is dedicated to the transport of folded proteins. The Tat system is now known to be essential for many bacterial processes including energy metabolism, cell wall biosynthesis, the nitrogen-fixing symbiosis and bacterial pathogenesis. Recent studies demonstrate that substrate-specific accessory proteins prevent improperly assembled substrates from interacting with the Tat transporter. During the transport cycle itself substrate proteins bind to a receptor complex in the membrane which then recruits a protein-translocating channel to carry out the transport reaction.
Arabidopsis RTNLB1 and RTNLB2 Reticulon-like proteins regulate intracellular trafficking and activity of the FLS2 immune...Arabidopsis RTNLB1 and RTNLB2 Reticulon-like proteins regulate intracellular trafficking and activity of the FLS2 immune...
Receptors localized at the plasma membrane are critical for the recognition of pathogens. The molecular determinants that regulate receptor transport to the plasma membrane are poorly understood. In a screen for proteins that interact with the FLAGELIN-SENSITIVE2 (FLS2) receptor using Arabidopsis thaliana protein microarrays, we identified the reticulon-like protein RTNLB1. We showed that FLS2 interacts in vivo with both RTNLB1 and its homolog RTNLB2 and that a Ser-rich region in the N-terminal tail of RTNLB1 is critical for the interaction with FLS2. Transgenic plants that lack RTNLB1 and RTNLB2 (rtnlb1 rtnlb2) or overexpress RTNLB1 (RTNLB1ox) exhibit reduced activation of FLS2-dependent signaling and increased susceptibility to pathogens. In both rtnlb1 rtnlb2 and RTNLB1ox, FLS2 accumulation at the plasma membrane was significantly affected compared with the wild type. Transient overexpression of RTNLB1 led to FLS2 retention in the endoplasmic reticulum (ER) and affected FLS2 glycosylation but ...
Tracy Palmer GroupTracy Palmer Group
The major research focus of my group is the transport of proteins by the twin arginine protein transport pathway. This pathway, which is found in the cytoplasmic membranes of most bacteria, and the thylakoid membranes of plant chloroplasts, is highly unusual because it transports pre-folded proteins. Protein substrates are targeted to the Tat machinery by N-terminal signal peptides that contain an S/T- R-R-x-F-L-K twin arginine motif. Our aims are to study the function and mechanism of the Tat protein transporter, and the contribution that it makes to the physiology of bacteria. The Gram-positive bacterium Staphylococcus aureus uses an unusual Type VII secretion system to secrete possible virulence factors. In a collaboration with Professor Bill Hunter we have been structurally and biochemically characterising components and substrates of this system. Contact details ...
ffh protein (Yersinia pseudotuberculosis) - STRING interaction networkffh protein (Yersinia pseudotuberculosis) - STRING interaction network
Protein translocase subunit SecY; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently (443 aa ...
Toponomics method for the automated quantification of membrane protein translocation | BMC Bioinformatics | Full TextToponomics method for the automated quantification of membrane protein translocation | BMC Bioinformatics | Full Text
Intra-cellular and inter-cellular protein translocation can be observed by microscopic imaging of tissue sections prepared immunohistochemically. A manual densitometric analysis is time-consuming, subjective and error-prone. An automated quantification is faster, more reproducible, and should yield results comparable to manual evaluation. The automated method presented here was developed on rat liver tissue sections to study the translocation of bile salt transport proteins in hepatocytes. For validation, the cholestatic liver state was compared to the normal biological state. An automated quantification method was developed to analyze the translocation of membrane proteins and evaluated in comparison to an established manual method. Firstly, regions of interest (membrane fragments) are identified in confocal microscopy images. Further, densitometric intensity profiles are extracted orthogonally to membrane fragments, following the direction from the plasma membrane to cytoplasm. Finally, several
LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum<...LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum<...
TY - JOUR. T1 - LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. AU - Tyson, John R. AU - Stirling, Colin J. PY - 2000. Y1 - 2000. N2 - Lhs1p is an Hsp70-related chaperone localized in the endoplasmic reticulum (ER) lumen. Δlhs1 mutant cells are viable but are constitutively induced for the unfolded protein response (UPR). Here, we demonstrate a severe growth defect in Δire1Δlhs1 double mutant cells in which the UPR can no longer be induced. In addition, we have identified a UPR- regulated gene, SIL1, whose overexpression is sufficient to suppress the Δire1Δlhs1 growth defect. SIL1 encodes an ER-localized protein that interacts directly with the ATPase domain of Kar2p (BiP), suggesting some role in modulating the activity of this vital chaperone. SIL1 is a non-essential gene but the Δlhs1Δsil1 double mutation is lethal and correlates with a complete block of protein translocation into the ER. We conclude that the ...
Selective Transport And Selective Retention Of Cargo - Synaptic PlasticitySelective Transport And Selective Retention Of Cargo - Synaptic Plasticity
Not all proteins that accumulate in a specific subcellular compartment undergo processes of selective sorting and transport. Some proteins seem to be localized by a mechanism known as selective retention, which describes that cargoes are transported nonselectively to both axons and dendrites, but are eliminated at one side by selective endocytosis and retained at the other, where endocytosis is prevented. Prominent examples for this process are the proteins VAMP2 and NgCAM. NgCAM is sorted into carriers that preferentially deliver their cargo proteins to the axonal membrane. In contrast, VAMP2 is delivered to the surface of both axons and dendrites; however it is preferentially endocytosed from the dendritic membrane, a process, which also results in an axonal enrichment31. Indeed, VAMP2 harbors an endocytosis signal in its cytoplasmic domain, and mutation of this sequence consistently results in an evenly distribution of VAMP2 to cell body, dendrites, and axon. Although such process initially ...
Rab6 Coordinates a Novel Golgi to ER Retrograde Transport Pathway in Live Cells | JCBRab6 Coordinates a Novel Golgi to ER Retrograde Transport Pathway in Live Cells | JCB
Our results are consistent with the idea that the FP-Rab6 membrane system defines a separate compartment that corresponds to a Golgi→ER transport pathway containing specific retrograde cargo and exhibiting distinct functional requirements. The FP-Rab6 compartment comprises all FP-Rab6 elements, the Golgi-associated pool, tubular and globular trafficking elements, and peripheral corner regions. It is separate from some of the traditionally defined morphological compartments (endosomes, lysosomes, and Golgi→plasma membrane transport carriers), and partly overlaps with others (Golgi, ER). FP-Rab6 dynamics in live cells emphasized elements that were neglected in static images, thus revealing morphological features of endogenous Rab6 that had previously been overlooked ( Goud et al. 1990; Antony et al. 1992). Since endogenous Rab6 and FP-Rab6 have common features ( Fig. 2), FP-Rab6 dynamics are most likely not induced by overexpression of the FP-Rab6 fusion protein.. During the period when STB ...
4v7e - Proteopedia, life in 3D4v7e - Proteopedia, life in 3D
The biogenesis of secretory as well as transmembrane proteins requires the activity of the universally conserved protein-conducting channel (PCC), the Sec61 complex (SecY complex in bacteria). In eukaryotic cells the PCC is located in the membrane of the endoplasmic reticulum where it can bind to translating ribosomes for co-translational protein transport. The Sec complex consists of three subunits (Sec61alpha, beta and gamma) and provides an aqueous environment for the translocation of hydrophilic peptides as well as a lateral opening in the Sec61alpha subunit that has been proposed to act as a gate for the membrane partitioning of hydrophobic domains. A plug helix and a so-called pore ring are believed to seal the PCC against ion flow and are proposed to rearrange for accommodation of translocating peptides. Several crystal and cryo-electron microscopy structures revealed different conformations of closed and partially open Sec61 and SecY complexes. However, in none of these samples has the ...
Sec31a - Protein transport protein Sec31A - Rattus norvegicus (Rat) - Sec31a gene & proteinSec31a - Protein transport protein Sec31A - Rattus norvegicus (Rat) - Sec31a gene & protein
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Tools for ESCRT protein studies - Visualising the invisibleTools for ESCRT protein studies - Visualising the invisible
Endosomal internalisation and subsequent lysosomal degradation of membrane proteins is important for regulation of multiple cellular processes, among these the termination of receptor signalling and degradation of misfolded membrane proteins. ESCRT (Endosomal sorting complex required for transport) proteins are vital for the sorting of ubiquitinated membrane proteins into multivesicular bodies for subsequent degradation in the lysosome. In this study we generated two stable cell lines expressing the EGFP tagged ESCRT proteins Hrs and hVps22. Our goal was to utilise these cell lines for investigations into ESCRT protein dynamics, the relative order of ESCRT protein recruitment to the endosomes, and the endosomal localisation of ESCRT proteins. However, though the EGFP-Hrs cell line seemed to express a functional Hrs protein, the EGFP-hVps22 protein was completely cytosolic and could not be visualised on endosomes. hVps4, and its mouse homologue Skd1 is an AAA-type ATPase shown to be necessary for ...
TRIM22 alters the sub-cellular localization of Gag prot | Open-iTRIM22 alters the sub-cellular localization of Gag prot | Open-i
TRIM22 alters the sub-cellular localization of Gag protein.A) Analysis of Gag localization by fluorescence microscopy. HOS-CD4/CXCR4 cells were co-transfected w
Axonal transportAxonal transport
The long length of axons makes them critically dependent on intracellular transport for their growth and survival. This movement is called axonal transport. Cargoes originating from the cell body move out towards the axon tip and cargoes originating in the axon or at the axon tip move back towards the cell body. The outbound movement is known as anterograde transport and it includes cargoes required for the growth, maintenance and plasticity of axons and presynaptic terminals. The inbound movement is called retrograde transport and it includes cargoes returning to the cell body for recycling or degradation, as well as cargoes that relay signals back to the cell body to modulate gene expression in response to the local environment.. Though axonal transport has a special name, it is not fundamentally different from the pathways of intracellular traffic found in other parts of nerve cells or in other cells. However, it is remarkable for its scale. For example, there are axons in our bodies that ...
The quest for a better resolution of protein‐translocation processes | EMBO ReportsThe quest for a better resolution of protein‐translocation processes | EMBO Reports
The most thoroughly characterized quality‐control system is the one operating in the ER, which is a compartment specialized in the folding and subsequent export of translocated proteins. Unfolded proteins are typically denied access to the export pathway until they fold correctly, and those that fail to do so are disposed of by a process known as ERAD. This involves the retrotranslocation (dislocation) of misfolded substrates from the lumen of the ER, across the ER membrane back into the cytosol, followed by their ubiquitination and degradation by the proteasome. Under stress conditions, in which the workload imposed on the ER exceeds its capacity, cells respond by increasing the transcription of genes coding for ER chaperones as well as for ERAD components, and by attenuating protein synthesis-the so‐called unfolded protein response. R.S. Hegde (Bethesda, MD, USA) and D. T. Ng (Singapore) reported on additional ways in which the secretory pathway can respond to stress.. Hegde discussed an ...
Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5pRecognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p
Peroxisomes require the translocation of folded and functional target proteins of various sizes across the peroxisomal membrane. We have investigated the structure and function of the principal import receptor Pex5p, which recognizes targets bearing a C-terminal peroxisomal targeting signal type 1. …
Proteins that are destined to become associated with the inner surface of the plasma membrane areProteins that are destined to become associated with the inner surface of the plasma membrane are
Listing of the answers to the question: Proteins that are destined to become associated with the inner surface of the plasma membrane are:
Dissolving protein traffic jam at the entrance of mitochondria - Institute of Biochemistry and Molecular BiologyDissolving protein traffic jam at the entrance of mitochondria - Institute of Biochemistry and Molecular Biology
Researchers from Freiburg discovered a novel mechanism that ensures obstacle-free protein traffic into the powerhouse of the cell
Webinar - Exosomes: New perspectives, tools, and technologies | Exosome RNAWebinar - Exosomes: New perspectives, tools, and technologies | Exosome RNA
Exosomes are tiny (30-150 nm) vesicles secreted by all cell types in culture and found in large numbers in all body fluids. These vesicles, loaded with unique RNA and protein cargo, have a wide range of biological functions, only a small part of which is currently understood. For example, they are known to serve as
SAUSA300 RS01830 - AureoWikiSAUSA300 RS01830 - AureoWiki
Genetic information processingProtein fateProtein and peptide secretion and traffickingTat (twin-arginine translocation) pathway signal sequence (TIGR01409; HMM-score: 25.5) ...
Melanoregulin, product of the dsu locus, links the BLOC-pathway and OA1 in organelle biogenesis. | Sigma-AldrichMelanoregulin, product of the dsu locus, links the BLOC-pathway and OA1 in organelle biogenesis. | Sigma-Aldrich
Sigma-Aldrich offers abstracts and full-text articles by [Rivka A Rachel, Kunio Nagashima, T Norene OSullivan, Laura S Frost, Frank P Stefano, Valeria Marigo, Kathleen Boesze-Battaglia].
mRNA & protein trafficking meeting | greenfluorescentblogmRNA & protein trafficking meeting | greenfluorescentblog
A meeting at the Weizmann Institute of Science in Israel, Nov 17-21, 2013. From their Welcome Letter: This meeting will bring together experts from the diverse fields of trafficking to discuss mechanisms of mRNA and protein transport, and their relationship to prominent diseases associated with organelle biogenesis. We hope to trigger significant scientific discourse between…
TIB - Notices - CTMTIB - Notices - CTM
Please, check the service warnings and service modifications on regular interurban transport routes in Majorca: bus, train, metro and public bicycle.
TIB - Notices - CTMTIB - Notices - CTM
Please, check the service warnings and service modifications on regular interurban transport routes in Majorca: bus, train, metro and public bicycle.
Characterizing the Presence and Sensitivity of the P2X7 Receptor in Different Compartments of the Gut - FullText - Journal of...Characterizing the Presence and Sensitivity of the P2X7 Receptor in Different Compartments of the Gut - FullText - Journal of...
Purinergic signaling has been established as an important feature of inflammation and homeostasis. The expression of a number of P2 receptor subtypes in the gut has been reported. In this study, using
Babraham Institute » EquipmentBabraham Institute » Equipment
The Imagestream is an image cytometer that allows quantitative data to be acquired as well as images of every event passing through the instrument to be recorded. This machine can analyse up to 5000 cells/sec. This clever machine allows the user to look at features of cells such as co-localisation, staining location, cell-cell location, spot counting and cell death analysis ...
Only JuicesOnly Juices
In developing our recipes, we choose only the very best raw materials from the world, with the most competitive prices; we organize the transport from any part of the world to the packaging plants and, once bottled we organize the transport to its final destination; we study the standards and seasonality of the products; we research and control supplies on a global scale to ensure raw material availability all year round.. ...
Completed - Pippy vs AlphaJolt 3v3ing! | Smogon ForumsCompleted - Pippy vs AlphaJolt 3v3ing! | Smogon Forums
Open Challenge! 3v3 singles 2 Day DQ 0 Recoveries, 5 Chills Arena Final Destination: Thats right, a battle at Final Dest. Just like in Brawl, if...
Cargo Compartment Essay - 299 WordsCargo Compartment Essay - 299 Words
CARGO COMPARTMENT CLASSIFICATION Class A The presence of a fire would be easily discovered by a crewmember while at his or her station and each part of
உயிரணுக்கணிகம் - தமிழ் விக்கிப்பீடியாஉயிரணுக்கணிகம் - தமிழ் விக்கிப்பீடியா
உயிரணு உயிரியலில் உயிரணுக்கணிகம் அல்லது கலக்கணிகம் அல்லது குழியவுரு (Cytoplasm) என்பது உயிரணு ஒன்றின் உள்ளடக்கத்தில், உயிரணுக் கரு தவிர்ந்த மிகுதியாக உள்ள பகுதியாகும். இது உயிரணு நீர்மம் (en:Cytosol) எனும் நீர்மக் கரைசலையும் (இந்த நீர்மக் கரைசல் உயிரணு மென்சவ்விற்கு உள்ளாக இருக்கும் கூழ்மப் பொருள்), உயிரணுக்களின் உள்ளே காணப்படும் நுண்ணுறுப்புக்களையும் உள்ளடக்கிய பகுதி ஆகும். இந்த ...
endoplasmic reticulumendoplasmic reticulum
ChloroplastChloroplast
ImportinImportin
International Max Planck Research School for Molecular and Cellular Life SciencesInternational Max Planck Research School for Molecular and Cellular Life Sciences
David E. ClemmerDavid E. Clemmer
Mitochondrial carrierMitochondrial carrier
CLCA1CLCA1
StAR-related transfer domainStAR-related transfer domain
CKAP4CKAP4
STS-52STS-52
Cochlear amplifierCochlear amplifier
ATP-binding domain of ABC transportersATP-binding domain of ABC transporters
EndoplasmEndoplasm
R. John EllisR. John Ellis
Cathepsin ACathepsin A
Crustacean neurohormone familyCrustacean neurohormone family
Isoelectric focusingIsoelectric focusing
RetromerRetromer
SYT3SYT3
Disulfide oxidoreductase DDisulfide oxidoreductase D
Calcium deficiency (plant disorder)Calcium deficiency (plant disorder)
NDUFA4NDUFA4
Cofactor (biochemistry)Cofactor (biochemistry)
Jared Diamond bibliographyJared Diamond bibliography
Partition coefficientPartition coefficient
SLC27A1SLC27A1
FABP7FABP7
Asparagine peptide lyaseAsparagine peptide lyase
NEFMNEFM
STS-73STS-73
Cell membrane - Simple English Wikipedia, the free encyclopediaCell membrane - Simple English Wikipedia, the free encyclopedia
LeafLeaf
EbolaEbola
OligosaccharyltransferaseOligosaccharyltransferase
GABRA4GABRA4
Chloroplast DNAChloroplast DNA
Endoplasmic reticulum - Simple English Wikipedia, the free encyclopediaEndoplasmic reticulum - Simple English Wikipedia, the free encyclopedia
Apolipoprotein C4Apolipoprotein C4
OctopusOctopus
SakeSake
PAX8PAX8
User:Flyguy649User:Flyguy649
DiagenesisDiagenesis
JouleJoule
QuercetinQuercetin
WhaleWhale
ReptileReptile
GABAA receptor positive allosteric modulatorGABAA receptor positive allosteric modulator
Wikipedia:Makala za msingi za kamusi elezo/Zote 1000, kamusi elezo huruWikipedia:Makala za msingi za kamusi elezo/Zote 1000, kamusi elezo huru
PastaPasta
NADH deshidroxenase, a enciclopedia libreNADH deshidroxenase, a enciclopedia libre
Hypervitaminosis AHypervitaminosis A
Starling equationStarling equation
PSEN1PSEN1
Competitive inhibitionCompetitive inhibition
Mineral (nutrient)Mineral (nutrient)
PicornavirusPicornavirus
Beta-glucanBeta-glucan
GingerGinger
TeaTea
AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesTechnology, Industry, AgricultureInformation ScienceHealth Care
Protein TransportBiological TransportGolgi ApparatusBiological Transport, ActiveMembrane Transport ProteinsBrefeldin AEndoplasmic ReticulumVesicular Transport ProteinsMembrane ProteinsIntracellular MembranesCarrier ProteinsAxonal TransportCathepsin ATransport VesiclesMolecular Sequence DataCoatomer ProteinAmino Acid SequenceIon TransportSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeVacuolesCell MembraneFungal ProteinsPeasCyclopentanestrans-Golgi NetworkProtein Sorting SignalsKineticsrab2 GTP-Binding ProteinMutationrab GTP-Binding ProteinsCell CompartmentationModels, BiologicalCOP-Coated VesiclesChloroplast ProteinsMonosaccharide Transport ProteinsThylakoidsbeta-FructofuranosidaseRecombinant Fusion ProteinsChloroplastsCoated VesiclesProteinsEndosomesProtein Processing, Post-TranslationalCoat Protein Complex ICell LineElectron TransportEndoplasmic Reticulum, RoughCytoplasmOrganellesrab1 GTP-Binding ProteinsHydrogen-Ion ConcentrationMicroscopy, ElectronProtein BindingADP-Ribosylation FactorsCarboxypeptidasesPlant ProteinsBacterial ProteinsAdenosine TriphosphatasesProtein PrecursorsMembrane GlycoproteinsSodiumNuclear Pore Complex ProteinsAdenosine TriphosphateCloning, MolecularEscherichia coli ProteinsEscherichia coliSequence Homology, Amino AcidGreen Fluorescent ProteinsEndocytosisBase SequenceADP-Ribosylation Factor 1Molecular ChaperonesActive Transport, Cell NucleusTemperatureMasoprocolran GTP-Binding ProteinGenes, FungalMelanotrophsProtein Structure, TertiaryViral Envelope ProteinsGlycosylationCytosolCricetinaeSubcellular FractionsMicrosomesClinical Chemistry TestsCells, CulturedGTP-Binding ProteinsCell NucleusMonensinMicroscopy, FluorescenceAnion Transport ProteinsDogsLuminescent ProteinsCation Transport ProteinsYeastsMicroscopy, ImmunoelectronQa-SNARE ProteinsRecombinant ProteinsDiffusionMicrotubulesN-Ethylmaleimide-Sensitive ProteinsGenetic Complementation TestAdaptor Proteins, Vesicular TransportHeLa CellsGlucoseCell FractionationGlycoside HydrolasesProton-Motive ForceProtein Synthesis InhibitorsSequence AlignmentAmino Acid Transport SystemsGuanine Nucleotide Exchange FactorsCHO CellsGTP PhosphohydrolasesNuclear EnvelopeTime FactorsMitochondriaGuanosine TriphosphateTransfectionModels, MolecularMonomeric GTP-Binding ProteinsChloridesLysosomesProtein ConformationPlasmidsNocodazoleReceptors, PeptideMitochondrial Membrane Transport ProteinsCell-Free SystemAlbuminsSymportersBinding SitesMethylglucosidesAdaptor Protein Complex 1Vesicular stomatitis Indiana virusRNA, MessengerCell PolarityPeptidesArabidopsisPhospholipid Transfer ProteinsSNARE Proteins3-O-MethylglucoseMutagenesis, Site-DirectedOvum TransportATP-Binding Cassette TransportersSignal Recognition ParticleMembrane FusionPlantsMacromolecular SubstancesClathrinDNA, ComplementaryFluorescent Antibody TechniqueAmino Acid Transport Systems, BasicMicrotubule-Associated ProteinsMicroscopy, ConfocalSignal TransductionPotassiumArabidopsis ProteinsNuclear ProteinsDNA PrimersRNA TransportAmino Acid Transport Systems, NeutralBlotting, WesternMethylglycosidesOrganic Cation Transport ProteinsCricetulusProton-Translocating ATPasesTwo-Hybrid System TechniquesGTPase-Activating ProteinsElectrophoresis, Polyacrylamide GelMicroinjectionsLiverPlant LeavesAmino AcidsHeat-Shock ProteinsPhenotypeArginineMolecular WeightGlucose Transport Proteins, FacilitativeExocytosisHSP70 Heat-Shock ProteinsNerve Tissue ProteinsEpithelial CellsAminoisobutyric AcidsMutagenesisDeoxyglucoseCOS CellsProtein BiosynthesisMicrovilliPhotosynthetic Reaction Center Complex ProteinsCell Membrane PermeabilityIntestinal AbsorptionPhloretinGene DeletionHydrolysisTransportationAnionsMembrane Transport ModulatorsGlycoproteins
Parkinsons disease : Alpha synucleins non-amyloidal component (NAC) aids the proteins movement through axons - https:/...Parkinson's disease : Alpha synuclein's non-amyloidal component (NAC) aids the protein's movement through axons - https:/...
Mechanisms of intracellular protein transport. - PubMed - NCBIMechanisms of intracellular protein transport. - PubMed - NCBI
Lipid Transport Protein [image] | EurekAlert! Science NewsLipid Transport Protein [image] | EurekAlert! Science News
Molecular mechanisms of nuclear protein transport. - PubMed - NCBIMolecular mechanisms of nuclear protein transport. - PubMed - NCBI
Airlock-like transport protein structure discovered | EurekAlert! Science NewsAirlock-like transport protein structure discovered | EurekAlert! Science News
Transport protein - WikipediaTransport protein - Wikipedia
Structure of the Iron Transport-Protein [image] | EurekAlert! Science NewsStructure of the Iron Transport-Protein [image] | EurekAlert! Science News
Which cellular organelle contains phospholipids chelosterol and transport protein - AnswersWhich cellular organelle contains phospholipids chelosterol and transport protein - Answers
Vesicular transport protein - WikipediaVesicular transport protein - Wikipedia
RNA transcription, translation and transport factor protein (IPR019265) | InterPro | EMBL-EBIRNA transcription, translation and transport factor protein (IPR019265) | InterPro | EMBL-EBI
Receptor-transporting protein 3 (Q9BQQ7) | InterPro | EMBL-EBIReceptor-transporting protein 3 (Q9BQQ7) | InterPro | EMBL-EBI
What Are Transport Proteins? | Reference.comWhat Are Transport Proteins? | Reference.com
Transport proteinTransport protein
glutamate/aspartate transport protein Protein Superfamily Detailglutamate/aspartate transport protein Protein Superfamily Detail
Hemoglobin Transport ProteinHemoglobin Transport Protein
Protein Sorting by Transport Vesicles | ScienceProtein Sorting by Transport Vesicles | Science
Mechanisms of Drug Interactions II: Transport Proteins | SpringerLinkMechanisms of Drug Interactions II: Transport Proteins | SpringerLink
Rhesus Proteins Transport Ions, not GasRhesus Proteins Transport Ions, not Gas
Heavily loaded transport protein catch-bonds : - AskNatureHeavily loaded transport protein catch-bonds : - AskNature
Structural model for the protein-translocating element of the twin-arginine transport system | PNASStructural model for the protein-translocating element of the twin-arginine transport system | PNAS
RCSB PDB - Protein Feature View - Magnesium transport protein CorA - Q9WZ31 (CORA THEMA)RCSB PDB - Protein Feature View - Magnesium transport protein CorA - Q9WZ31 (CORA THEMA)
The Cdc25 protein of Saccharomyces cerevisiae is required for normal glucose transportThe Cdc25 protein of Saccharomyces cerevisiae is required for normal glucose transport
H(+)-transporting V0 sector ATPase subunit d [Saccharomyces cerevisiae - Protein - NCBIH(+)-transporting V0 sector ATPase subunit d [Saccharomyces cerevisiae - Protein - NCBI
Researchers find new molecular motors that bacteria use to transport proteinsResearchers find new 'molecular motors' that bacteria use to transport proteins
Multidrug resistance associated protein 2 mediates transport of prostaglandin E2Multidrug resistance associated protein 2 mediates transport of prostaglandin E2
Transport Phenomena and Protein Stability in Downstream Processing of Biopharmaceuticals-Chemical Engineering - Carnegie Mellon...Transport Phenomena and Protein Stability in Downstream Processing of Biopharmaceuticals-Chemical Engineering - Carnegie Mellon...
RCSB PDB - Protein Feature View - Band 3 anion transport protein - P02730 (B3AT HUMAN)RCSB PDB - Protein Feature View - Band 3 anion transport protein - P02730 (B3AT HUMAN)
Current Topics in Membranes & Transport Vol. 36: Protein-Membrane Interactions: : 9780121533366: Powells BooksCurrent Topics in Membranes & Transport Vol. 36: Protein-Membrane Interactions: : 9780121533366: Powell's Books
CLM82 25905 - Transport permease protein - Streptomyces albidoflavus - CLM82 25905 gene & proteinCLM82 25905 - Transport permease protein - Streptomyces albidoflavus - CLM82 25905 gene & protein
Sec31a - Protein transport protein Sec31A - Rattus norvegicus (Rat) - Sec31a gene & proteinSec31a - Protein transport protein Sec31A - Rattus norvegicus (Rat) - Sec31a gene & protein
AnatomyOrganismsChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesTechnology, Industry, AgricultureInformation ScienceHealth Care
Protein TransportBiological TransportGolgi ApparatusBiological Transport, ActiveMembrane Transport ProteinsBrefeldin AEndoplasmic ReticulumVesicular Transport ProteinsMembrane ProteinsIntracellular MembranesCarrier ProteinsAxonal TransportCathepsin ATransport VesiclesMolecular Sequence DataCoatomer ProteinAmino Acid SequenceIon TransportSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeVacuolesCell MembraneFungal ProteinsPeasCyclopentanestrans-Golgi NetworkProtein Sorting SignalsKineticsrab2 GTP-Binding ProteinMutationrab GTP-Binding ProteinsCell CompartmentationModels, BiologicalCOP-Coated VesiclesChloroplast ProteinsMonosaccharide Transport ProteinsThylakoidsbeta-FructofuranosidaseRecombinant Fusion ProteinsChloroplastsCoated VesiclesProteinsEndosomesProtein Processing, Post-TranslationalCoat Protein Complex ICell LineElectron TransportEndoplasmic Reticulum, RoughCytoplasmOrganellesrab1 GTP-Binding ProteinsHydrogen-Ion ConcentrationMicroscopy, ElectronProtein BindingADP-Ribosylation FactorsCarboxypeptidasesPlant ProteinsBacterial ProteinsAdenosine TriphosphatasesProtein PrecursorsMembrane GlycoproteinsSodiumNuclear Pore Complex ProteinsAdenosine TriphosphateCloning, MolecularEscherichia coli ProteinsEscherichia coliSequence Homology, Amino AcidGreen Fluorescent ProteinsEndocytosisBase SequenceADP-Ribosylation Factor 1Molecular ChaperonesActive Transport, Cell NucleusTemperatureMasoprocolran GTP-Binding ProteinGenes, FungalMelanotrophsProtein Structure, TertiaryViral Envelope ProteinsGlycosylationCytosolCricetinaeSubcellular FractionsMicrosomesClinical Chemistry TestsCells, CulturedGTP-Binding ProteinsCell NucleusMonensinMicroscopy, FluorescenceAnion Transport ProteinsDogsLuminescent ProteinsCation Transport ProteinsYeastsMicroscopy, ImmunoelectronQa-SNARE ProteinsRecombinant ProteinsDiffusionMicrotubulesN-Ethylmaleimide-Sensitive ProteinsGenetic Complementation TestAdaptor Proteins, Vesicular TransportHeLa CellsGlucoseCell FractionationGlycoside HydrolasesProton-Motive ForceProtein Synthesis InhibitorsSequence AlignmentAmino Acid Transport SystemsGuanine Nucleotide Exchange FactorsCHO CellsGTP PhosphohydrolasesNuclear EnvelopeTime FactorsMitochondriaGuanosine TriphosphateTransfectionModels, MolecularMonomeric GTP-Binding ProteinsChloridesLysosomesProtein ConformationPlasmidsNocodazoleReceptors, PeptideMitochondrial Membrane Transport ProteinsCell-Free SystemAlbuminsSymportersBinding SitesMethylglucosidesAdaptor Protein Complex 1Vesicular stomatitis Indiana virusRNA, MessengerCell PolarityPeptidesArabidopsisPhospholipid Transfer ProteinsSNARE Proteins3-O-MethylglucoseMutagenesis, Site-DirectedOvum TransportATP-Binding Cassette TransportersSignal Recognition ParticleMembrane FusionPlantsMacromolecular SubstancesClathrinDNA, ComplementaryFluorescent Antibody TechniqueAmino Acid Transport Systems, BasicMicrotubule-Associated ProteinsMicroscopy, ConfocalSignal TransductionPotassiumArabidopsis ProteinsNuclear ProteinsDNA PrimersRNA TransportAmino Acid Transport Systems, NeutralBlotting, WesternMethylglycosidesOrganic Cation Transport ProteinsCricetulusProton-Translocating ATPasesTwo-Hybrid System TechniquesGTPase-Activating ProteinsElectrophoresis, Polyacrylamide GelMicroinjectionsLiverPlant LeavesAmino AcidsHeat-Shock ProteinsPhenotypeArginineMolecular WeightGlucose Transport Proteins, FacilitativeExocytosisHSP70 Heat-Shock ProteinsNerve Tissue ProteinsEpithelial CellsAminoisobutyric AcidsMutagenesisDeoxyglucoseCOS CellsProtein BiosynthesisMicrovilliPhotosynthetic Reaction Center Complex ProteinsCell Membrane PermeabilityIntestinal AbsorptionPhloretinGene DeletionHydrolysisTransportationAnionsMembrane Transport ModulatorsGlycoproteins
InsightsNormalMembranesTransportersTranslocationMechanismPathwayFamily of proteinsVesiclesIonsMolecularCytoplasmKinasePeptidesAbstractPrecursor proteinsPrecursorsTranslocaseSynthesisMRNACytosolicGeneTransmembrane proteinCellularIntracellular signalinSecretoryMaterials within an organismMechanismsTransporter proteinsAntigenPlasma membraneAntibodiesNucleusPathwaysCofactor-containiMitochondrial proteinsSequenceCopper Transport ProteinsNuclearSkeletal muscleCompartmentsEndoplasmicSubstancesATPasePreferentiallyCell'sMetabolismVesicular transportSubcellular localizationKnown transport proteinsUniversity of GroninAmino AcidsMediatesIntraflagellar transport proteinCellsGlucoseCellMultidrug resistaRegulationOuter membraneInhibitorsRegulateMembrane TransportMammalianMitochondriaChannel proteins
Insights1
  • Research by University at Buffalo biologists is providing new insights into alpha-synuclein, a small acidic protein associated with Parkinson's disease. (debuglies.com)
Normal1
  • The scientists found that when the larvae are engineered to produce both excess alpha-synuclein and a version of alpha-synuclein with the NAC region missing, the larvae crawl normally, the protein doesn't aggregate, and the synapses are normal. (debuglies.com)
Membranes23
Transporters10
Translocation13
Mechanism14
Pathway27
Family of proteins4
Vesicles8
Ions6
Molecular12
Cytoplasm7
Kinase6
  • In addition to a defect in glucose uptake, the cdc25-5 mutant strain exhibited differences in glucose metabolism, probably due to the decreased cAMP level and hence decreased protein kinase A activity. (nih.gov)
  • It has been hypothesized on the basis of studies on BC3H-1 myocytes that diacylglycerol generation with activation of protein kinase C (PKC) is involved in the stimulation of glucose transport in muscle by insulin. (osti.gov)
  • We have hypothesized that the 5′AMP-activated protein kinase (AMPK) functions as a signaling intermediary in exercise-stimulated glucose uptake. (diabetesjournals.org)
  • The phosphatidylinositol 3-kinase (PI 3-kinase) inhibitor wortmannin completely blocked insulin-stimulated transport, but did not inhibit AICAR- or contraction-stimulated transport. (diabetesjournals.org)
  • The PINOID gene was recently cloned and found to encode a protein-serine/threonine kinase. (biologists.org)
  • Here we show that the PINOID gene is inducible by auxin and that the protein kinase is present in the primordia of cotyledons, leaves and floral organs and in vascular tissue in developing organs or proximal to meristems. (biologists.org)
Peptides3
Abstract1
  • article{4103eda6-97a4-45fe-8b8c-d30ec247d415, abstract = {Many of the core proteins in Photosystem II (PS II) undergo reversible phosphorylation. (lu.se)
Precursor proteins5
Precursors2
Translocase3
Synthesis8
MRNA15
  • Perez-Gonzalez A, Rodriguez A, Huarte M, Salanueva IJ, Nieto A. hCLE/CGI-99, a human protein that interacts with the influenza virus polymerase, is a mRNA transcription modulator. (ebi.ac.uk)
  • Transport of mRNA to distal compartments in neurons, such as growth cones and dendritic spines, ensures local translation of proteins in response to receptor signaling. (jneurosci.org)
  • its contribution to the trafficking of mRNA binding proteins important for mRNA localization is not well understood. (jneurosci.org)
  • Myelin basic protein (MBP) mRNA is localized to myelin produced by oligodendrocytes of the central nervous system. (rupress.org)
  • MBP mRNA microinjected into oligodendrocytes in primary culture is assembled into granules in the perikaryon, transported along the processes, and localized to the myelin compartment. (rupress.org)
  • In this work, microinjection of various deleted and chimeric RNAs was used to delineate regions in MBP mRNA that are required for transport and localization in oligodendrocytes. (rupress.org)
  • The results indicate that transport requires a 21-nucleotide sequence, termed the RNA transport signal (RTS), in the 3′ UTR of MBP mRNA. (rupress.org)
  • Insertion of the RTS from MBP mRNA into nontransported mRNAs, causes the RNA to be transported to the oligodendrocyte processes. (rupress.org)
  • If the coding region of the mRNA is deleted, the RLR is no longer required for localization, and the region between nucleotide 667 and 953, containing the RTS, is sufficient for both RNA transport and localization. (rupress.org)
  • This provided evidence that mRNA encoding a protein synthesized on free polysomes was spatially localized within the cell. (rupress.org)
  • Transport and localization of exogenous myelin basic protein mRNA microinjected into oligodendrocytes. (rupress.org)
  • We have studied transport and localization of MBP mRNA in oligodendrocytes in culture by microinjecting labeled mRNA into living cells and analyzing the intracellular distribution of the injected RNA by confocal microscopy. (rupress.org)
  • Within minutes, the RNA forms granules which, in the case of MBP mRNA, are transported down the processes to the periphery of the cell where the distribution again becomes dispersed. (rupress.org)
  • This work represents the first characterization of intracellular movement of mRNA in living cells, and the first description of the role of RNA granules in transport and localization of mRNA in cells. (rupress.org)
  • Further investigation into the regulation of αENaC by Per1 revealed that cortical αENaC mRNA was reduced in Per1 KO mice, and Per1 knockdown resulted in reduced αENaC protein levels in immortalized murine renal cortical CD (CCD) mpkCCD c14 cells. (ahajournals.org)
Cytosolic3
  • In addition to Cu acquisition, SPL7 triggers the expression of various microRNAs, denoted Cu-microRNAs, which promote the degradation of the transcripts encoding for dispensable Cu-utilizing proteins, including cytosolic Cu/Zn-SOD ( CSD1 ), chloroplast stroma Cu/Zn-SOD ( CSD2 ), several laccases, and plantacyanin [ 9 , 14 - 16 ]. (hindawi.com)
  • Thereby, Xdj1 promotes the transfer of precursory proteins from the cytosolic chaperones to the TOM complex to initiate their import into the mitochondria . (phys.org)
  • Recruitment of Cytosolic J-Proteins by TOM Receptors Promotes Mitochondrial Protein Biogenesis, Cell Reports (2018). (phys.org)
Gene8
  • You can select a given mouse superfamily member and download (or forward to NCBI BLAST) FASTA formatted protein sequences of that mouse gene and its mouse, human and rat homologs, as defined in the corresponding HomoloGene Class. (jax.org)
  • p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence. (uniprot.org)
  • section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. (uniprot.org)
  • One of these polypeptides, termed Erv14p (ER-vesicle protein of 14 kD), corresponds to an open reading frame on yeast chromosome VII that is predicted to encode an integral membrane protein and shares sequence identity with the Drosophila cornichon gene product. (psu.edu)
  • p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors. (uniprot.org)
  • 4 Circadian clock proteins interact with E-box response elements in target gene promoters to affect transcriptional regulation. (ahajournals.org)
  • This gene encodes a member of the WD repeat protein family. (antibodies-online.com)
  • Death-associated protein 6 also known as Daxx is a protein that in humans is encoded by the DAXX gene. (wikipedia.org)
Transmembrane protein2
Cellular12
Intracellular signalin1
Secretory3
Materials within an organism2
Mechanisms6
Transporter proteins1
  • Half a century later this idea has turned into one of the most studied of all transporter proteins (SGLT1), the sodium-glucose cotransporter. (wikidoc.org)
Antigen3
  • The BK virus genome encodes three regulatory proteins, large and small tumor-antigen and the agnoprotein, as well as the capsid proteins VP1 to VP3. (sigmaaldrich.com)
  • The lipid A-core moiety and the O-antigen repeat units are synthesized at the cytoplasmic face of the IM and are separately exported via two independent transport systems, namely, the O-antigen transporter Wzx ( 13 , 17 ) and the ATP binding cassette (ABC) transporter MsbA that flips the lipid A-core moiety from the inner leaflet to the outer leaflet of the IM ( 12 , 28 , 45 ). (asm.org)
  • It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1 (ETS1). (wikipedia.org)
Plasma membrane2
Antibodies2
Nucleus10
  • Transport of proteins into and out of the nucleus occurs through nuclear pore complexes (NPC). (nih.gov)
  • Two additional proteins, the GTPase Ran and p10, are required to translocate the docked NLS protein into the nucleus. (nih.gov)
  • The retina projects proteins into more than 30 different areas of the central nervous system, but for the study, her team chose to evaluate the two major targets: the superior colliculus (which analyzes motion in the visual field and controls goal-directed head and eye movements), and the lateral geniculate nucleus (which analyzes the shape of objects we see and sends that information to a higher brain area, the visual cortex). (innovations-report.com)
  • These are proteins that are usually in the nucleus of a cell, but we found them far, far away from the nucleus, participating in some form of communication. (innovations-report.com)
  • Transport of maize streak virus (MSV) DNA into the nucleus of host cells is essential for virus replication and the presence of virus particles in the nuclei of infected cells implies that coat protein (CP) must enter the nucleus. (apsnet.org)
  • Both ss and ds DNA moved into the nucleus when co-injected with the CP but not with E. coli proteins alone. (apsnet.org)
  • These results suggest that, in addition to entering the nucleus where it is required for encapsidation of the viral ss DNA, the MSV CP facilitates the rapid transport of viral (ss or ds) DNA into the nucleus. (apsnet.org)
  • Although some of these nucleus-bound cargoes are essential for life, others cause disease, and researchers have been looking for ways to disrupt the transport chain that can fuel infection and cancer alike. (jefferson.edu)
  • Most importins, like the importin a1, tow upwards of 500-600 different proteins into the nucleus. (jefferson.edu)
  • ASK1 will be transported to the nucleus when UV-irradiation is used to treat the cell. (wikipedia.org)
Pathways3
  • Pathways for water and plasma proteins across the endothelial barrier that may be regulated by ANP. (jci.org)
  • A ) Pathways for plasma protein transport across the endothelial permeability barrier that ANP may modulate, including water and plasma transport through the interendothelial cleft at sites where there are infrequent breaks in the junctional strand (see refs. (jci.org)
  • In conclusion, the bidirectional transport of glutamine, glutamate, and aspartate by SLC38A10, and the immunostaining detected in neurons and astrocytes, suggest that SLC38A10 plays a role in pathways involved in neurotransmission. (diva-portal.org)
Cofactor-containi1
  • A related system operates in bacteria, apparently for the export of redox cofactor-containing proteins. (asknature.org)
Mitochondrial proteins3
Sequence11
  • A heterodimeric protein complex, composed of karyopherin alpha and beta (or importin alpha and beta) functions to target proteins containing a nuclear localization sequence (NLS) to the NPCs. (nih.gov)
  • The number of protein sequences returned does not always match the numbers of homologs shown, because the same protein sequence can be associated with multiple homologs. (jax.org)
  • For mouse superfamily members not included in any HomoloGene Class, only the mouse protein sequence is returned. (jax.org)
  • View conserved domains detected in this protein sequence using CD-search. (nih.gov)
  • Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed. (uniprot.org)
  • Despite exceptional sequence diversity, S-layer proteins (SLPs) share important characteristics such as their ability to form crystalline sheets punctuated with nano-scale pores, and their propensity for charged amino acids, leading to acidic or basic isoelectric points. (nature.com)
  • In response to Cu limitation, Arabidopsis master Cu homeostasis regulator SPL7 (SQUAMOSA promoter-binding protein-like 7), similar to Chlamydomonas reinhardtii Crr1 transcription factor [ 8 ], activates the expression of multiple genes that contain within their promoter repetitive Cu-responsive elements (CuREs) with a GTAC motif as the essential core sequence [ 9 - 11 ]. (hindawi.com)
  • The [ 3 H]LTC 4 -labeled 190-kilodalton protein was immunoprecipitated by an antiserum against the COOH-terminal sequence of multidrug resistance-associated protein. (aacrjournals.org)
  • The multifunctional RNA-binding protein Tudor-SN plays multiple roles in transcriptional and posttranscriptional processes due to its modular domain structure, consisting of four tandem Staphylococcus nuclease (SN)-like domains (4SN), followed by a carboxyl-terminal Tudor domain, followed by a fifth partial SN sequence (Tsn). (plantphysiol.org)
  • Researchers reveal that the protein RCC1's overall structure, not its distinct amino acid sequence, determines whether it's fast-tracked into nuclei. (jefferson.edu)
  • Retention within the lumen of the ER correlates with an additional signal located at the C terminus, represented by the sequence Lys-Asp-Glu-Leu, known to be responsible for preventing secretion of proteins from the lumen of the ER in eukaryotic cells. (wikipedia.org)
Copper Transport Proteins1
  • In this project, the first goal is to design a plan to extend already successful in vitro biophysical research on copper transport proteins to (1) zinc and manganese transport proteins, for which less is known, and to (2) in vivo conditions exploring diseases related to problems with metal transport. (stias.ac.za)
Nuclear6
  • Thylakoids require the coordinated expression of both nuclear- and plastid-encoded proteins to allow rapid response to changing environmental conditions. (springer.com)
  • and proteins that play a direct role in the transport of karyopherin complexes through the nuclear pore complex. (harvard.edu)
  • Mutagenesis of a potential nuclear localization signal in the CP resulted in cytoplasmic accumulation of the mutant protein. (apsnet.org)
  • To investigate if CP might also be involved in viral DNA nuclear transport, Escherichia coli -expressed CP, together with TOTO-1-labeled viral ss or ds DNA, was microinjected into maize and tobacco epidermal cells. (apsnet.org)
  • The importin a3 molecule, or "car," is one of a family of importin proteins that help ferry other proteins across the nuclear membrane where they can alter the course of DNA transcription. (jefferson.edu)
  • Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. (wikipedia.org)
Skeletal muscle6
Compartments2
Endoplasmic3
Substances5
ATPase1
Preferentially1
Cell's1
Metabolism4
Vesicular transport8
Subcellular localization2
Known transport proteins1
  • The SemiSWEETs, among the smallest known transport proteins, assemble in pairs, thereby creating a structure that looks like their bigger plant and human SWEET homologs. (eurekalert.org)
University of Gronin2
  • Scientists at the University of Groningen studied the structure of a transport system that allows bacteria to pick up aspartate, a building block for proteins, from their environment. (rug.nl)
  • The structure of a transport complex used by bacteria to import aspartate has been mapped in unique detail by University of Groningen scientists. (rug.nl)
Amino Acids1
Mediates3
Intraflagellar transport protein1
  • We have identified sister of open brain ( sopb ), a null allele of mouse Intraflagellar transport protein 122 ( Ift122 ). (pnas.org)
Cells14
  • These sugars are taken up into cells, no matter whether these are bacteria, yeast, human cells or plant cells, by proteins that create sugar-specific pores in the membrane that surrounds a cell. (eurekalert.org)
  • In mammals, Rhesus proteins regulate acid and ion balance in kidney and liver cells. (innovations-report.com)
  • Defective transport of carbohydrates into cells is associated with a range of disorders, including cystic fibrosis, hypercholesterolemia, and diabetes. (indiatimes.com)
  • And at the root of all eye-to-brain communication are the hundreds of proteins generated by the retina's nerve cells. (innovations-report.com)
  • Using this new method--developed over the course of several years--Cline's team was able to "label" about 1,000 different types of proteins that originate in the eye's retinal ganglion cells, and then watch how and where they travel in a living brain of a rat. (innovations-report.com)
  • This can help us study what happens when a person experiences nerve damage and vision loss--and will hopefully lead us to treatments that can enhance protein transport and prevent cells from dying. (innovations-report.com)
  • The latter is also important for humans: we have a very similar transport system in our brain that plays a vital role in effective communication between brain cells. (rug.nl)
  • Such protein aggregates can be detrimental for cells and are thought to underlie the development of many diseases. (phys.org)
  • Immunohistochemical analysis of the gw/gw cochlea showed loss of the tight junction protein CLDN11 in strial basal cells from E40, loss of the potassium channel subunit KCNJ10 in strial intermediate cells from E50, and loss of the Na-K-Cl cotransporter SLC12A2 in strial marginal cells from E50. (wiley.com)
  • As part of a study to determine the function of primary cilia in lens we investigated the role of a key component of the intraflagellar transport (IFT) complex, IFT88, in cilia assembly in lens cells. (arvojournals.org)
  • In mice conditionally deficient for IFT88, the protein was absent from most lens cells, although a few scattered cells did show some reactivity. (arvojournals.org)
  • This supports tumor growth and metastasis as the exported lactate is taken up into other cancer cells by another transport protein (MCT1), where it serves as fuel. (myscience.ch)
  • BKV agnoprotein and α-SNAP were found to partially co-localize in cells, and a complex consisting of agnoprotein and α-SNAP could be co-immunoprecipitated from cells ectopically expressing the proteins as well as from BKV-transfected cells. (sigmaaldrich.com)
  • All the characteristic features of L-arginine transport displayed by the reconstituted system were similar to those observed in intact cells. (labome.org)
Glucose6
Cell9
  • Recent advances in understanding the machinery of vesicle transport have established general principles that underlie a broad variety of physiological processes, including cell surface growth, the biogenesis of distinct intracellular organelles, endocytosis, and the controlled release of hormones and neurotransmitters. (sciencemag.org)
  • Alcock F, Baker MA, Greene NP, Palmer T, Wallace MI, Berks BC (2013) Live cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system. (springer.com)
  • A new study from Scripps Research , which appears this month in Cell Reports , examines these proteins in unprecedented detail--providing surprising new insights into how visual signals are distributed to different regions of the brain. (innovations-report.com)
  • Because this type of neuronal protein exists in other parts of the body, it may play a role in other nerve-cell communication disorders such as Charcot-Marie-Tooth disease. (innovations-report.com)
  • Live cell imaging of mCherryZBP1 in neurons expressing GTD showed an increase in the number of motile particles, run length, and stimulated anterograde moving ZBP1 particles, suggesting that MyoVa controls availability of ZBP1 for microtubule-dependent transport. (jneurosci.org)
  • Aspartate is picked up from the environment, transported through the cell membrane and released on the inside of the cell. (rug.nl)
  • Homologous sequences are present in several other localized mRNAs, suggesting that the RTS represents a general transport signal in a variety of different cell types. (rupress.org)
  • In order to function properly, mitochondria are dependent on roughly 1,000 kinds of proteins, which are imported from the cytosol, the fluid inside the cell. (phys.org)
  • In this study, Dr. Cingolani's "cargo" was the RCC1 protein, which has a multitude of functions in the cell, and without which, the cell dies. (jefferson.edu)
Multidrug resista1
Regulation5
  • In vitro and in vivo measurement of defined cargoes and motors indicated that opposing motors are simultaneously engaged on cargoes that undergo bidirectional transport and suggest a potential for regulation during activation by controlling motor type and number. (jneurosci.org)
  • It could be proposed therefore that directed ZBP1 transport is carried out by and requires a fine-tuned regulation of multiple microtubule and actin motors. (jneurosci.org)
  • The current study aimed to investigate radiation-induced regulation of iron proteins including ferritin subunits in rats. (hindawi.com)
  • The circadian clock protein period 1 (Per1) contributes to the regulation of expression of the α subunit of the renal epithelial sodium channel at the basal level and in response to the mineralocorticoid hormone aldosterone. (ahajournals.org)
  • These data support a role for the circadian clock protein Per1 in the coordinate regulation of genes involved in renal sodium reabsorption. (ahajournals.org)
Outer membrane2
Inhibitors3
  • The researchers also investigated the transport properties of SfMCT and possible binding sites for inhibitors. (myscience.ch)
  • Both meristem organisation and growth of the primary root were rescued when seedlings were grown in the presence of polar auxin transport inhibitors, such as naphthylphtalamic acid (NPA). (biologists.org)
  • Treatment of seedlings or plant tissues with inhibitors of this polar auxin transport (PAT), such as naphthylphtalamic acid (NPA) or 2,3,5,-triiodo-benzoic acid (TIBA), showed that PAT provides directional and positional information for developmental processes such as vascular differentiation, apical dominance, organ development and tropic growth. (biologists.org)
Regulate1
Membrane Transport2
Mammalian1
Mitochondria3
Channel proteins1
Gli2 and Gli3 Localize to Cilia and Require the Intraflagellar Transport Protein Polaris for Processing and Function
Gli2 and Gli3 Localize to Cilia and Require the Intraflagellar Transport Protein Polaris for Processing and Function (journals.plos.org)
Correction of Chloride Transport and Mislocalization of CFTR Protein by Vardenafil in the Gastrointestinal Tract of Cystic...
Correction of Chloride Transport and Mislocalization of CFTR Protein by Vardenafil in the Gastrointestinal Tract of Cystic... (journals.plos.org)
Lipid Transport Protein [image] | EurekAlert! Science News
Lipid Transport Protein [image] | EurekAlert! Science News (eurekalert.org)
Airlock-like transport protein structure discovered | EurekAlert! Science News
Airlock-like transport protein structure discovered | EurekAlert! Science News (eurekalert.org)
Cellular mechanism may change cancer treatment
Cellular mechanism may change cancer treatment (medicalnewstoday.com)
Structures: Band 3 anion transport protein (P02730) | InterPro | EMBL-EBI
Structures: Band 3 anion transport protein (P02730) | InterPro | EMBL-EBI (ebi.ac.uk)
Structure of the Iron Transport-Protein [image] | EurekAlert! Science News
Structure of the Iron Transport-Protein [image] | EurekAlert! Science News (eurekalert.org)
Russell Diefenbach - Mendeley
Russell Diefenbach - Mendeley (mendeley.com)
Mitochondria and Medicine: The 2017 Dr. Paul Janssen Award Symposium | The New York Academy of Sciences
Mitochondria and Medicine: The 2017 Dr. Paul Janssen Award Symposium | The New York Academy of Sciences (nyas.org)
The structural basis for CD36 binding by the malaria parasite | Nature Communications
The structural basis for CD36 binding by the malaria parasite | Nature Communications (nature.com)
Endoplasmic reticulum
Endoplasmic reticulum (en.wikipedia.org)
Shannon Kelleher, Penn State [image] | EurekAlert! Science News
Shannon Kelleher, Penn State [image] | EurekAlert! Science News (eurekalert.org)
Merging cultures in the study of membrane traffic | Nature Cell Biology
Merging cultures in the study of membrane traffic | Nature Cell Biology (nature.com)
Frontiers | Inducing the Alternative Oxidase Forms Part of the Molecular Strategy of Anoxic Survival in Freshwater Bivalves |...
Frontiers | Inducing the Alternative Oxidase Forms Part of the Molecular Strategy of Anoxic Survival in Freshwater Bivalves |... (frontiersin.org)
Inhibiting the iron transport could halt tuberculosis
Inhibiting the iron transport could halt tuberculosis (news-medical.net)
JCI - Small intestine hexose transport in experimental diabetes. Increased transporter mRNA and protein expression in...
JCI - Small intestine hexose transport in experimental diabetes. Increased transporter mRNA and protein expression in... (jci.org)
IFT81 Gene - GeneCards | IFT81 Protein | IFT81 Antibody
IFT81 Gene - GeneCards | IFT81 Protein | IFT81 Antibody (genecards.org)
Tetratricopeptide repeat protein protects photosystem I from oxidative disruption during assembly | PNAS
Tetratricopeptide repeat protein protects photosystem I from oxidative disruption during assembly | PNAS (pnas.org)
Small Molecule Stabilizers as a Potential Treatment for Transthyretin Familial Amyloid Polyneuropathy | NIDDK
Small Molecule Stabilizers as a Potential Treatment for Transthyretin Familial Amyloid Polyneuropathy | NIDDK (niddk.nih.gov)
Chemistry News Articles: Chemistry 2011.org
Chemistry News Articles: Chemistry 2011.org (chemistry2011.org)
Protein Sorting by Transport Vesicles | Science
Protein Sorting by Transport Vesicles | Science (science.sciencemag.org)