0000000000326313

AUTHOR

Inmaculada Contreras

showing 4 related works from this author

Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.

2004

The ability of the cytosolic tail of a plant p24 protein to bind COPI and COPII subunits from plant and animal sources in vitro has been examined. We have found that a dihydrophobic motif in the -7,-8 position (relative to the cytosolic carboxy-terminus), which strongly cooperates with a dilysine motif in the -3,-4 position for COPI binding, is required for COPII binding. In addition, we show that COPI and COPII coat proteins from plant cytosol compete for binding to the sorting motifs in these tails. Only in the absence of the dilysine motif in the -3,-4 position or after COPI depletion could we observe COPII binding to the p24 tail. This competition is not observed when using rat liver cy…

CoatPhysiologyAmino Acid MotifsArabidopsisReceptors Cytoplasmic and NuclearPlant ScienceBiologyCoat Protein Complex ICytosolAnimalsCOPIIBinding SitesVesicular-tubular clusterArabidopsis ProteinsCell BiologyGeneral MedicineCOPIPlant cellIn vitroPeptide FragmentsCell biologyRatsCytosolProtein TransportRat liverCOP-Coated VesiclesProtein BindingSignal TransductionPlantcell physiology
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Characterization of Cop I Coat Proteins in Plant Cells

2000

Membrane traffic in eukaryotic cells is mediated by COP (coat protein)-coated vesicles. Their existence in plant cells has not yet been unequivocally demonstrated, although coated vesicles (probably with a COP coat) can be seen by electron microscopy. At the gene level, plant cells seem to contain all the components necessary to form COP-coated vesicles. In this paper, we have used antibodies raised against mammalian COPI coat proteins to detect putative homologues in rice (Oryza sativa) cells. Using these antibodies, we have found that rice cells contain alpha-, beta-, beta'-, and gamma-COP, as well as ADP-ribosylation factor (ARF) 1 protein. In addition, we show that antibodies against ma…

ImmunoprecipitationBlotting WesternBiophysicsCoated vesicleCross ReactionsBiologyCoatomer ProteinBiochemistryAntibodiesCytosolMicrosomesAnimalsMolecular BiologyVesiclefood and beveragesBiological TransportNeomycinOryzaCell BiologyCOPIPlant cellPrecipitin TestshumanitiesRatsCell biologyMolecular WeightCytosolLiverBiochemistryCoatomerbiology.proteinADP-Ribosylation Factor 1Guanosine TriphosphateAntibodyProtein BindingBiochemical and Biophysical Research Communications
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Uptake of endocytic markers by rice cells: variations related to the growth phase.

2001

Endocytosis is now considered a basic cellular process common to plant cells. Although both non-specific and receptor-mediated endocytosis appear to take place in plant cells, the physiological role of the latter remains unclear. We have investigated the endocytic process in rice cell suspensions using two biotinylated proteins, peroxidase and bovine serum albumin (bHRP and bBSA), as markers. First, we show that markers are internalized by rice cells and appear in intracellular membranes. The uptake of the two markers is temperature dependent, saturable with time and markers dose and it is competed by free biotin. Thus, it shows the properties of a receptor-mediated process. We also show th…

HistologyEndocytic cycleCellSerum albuminBiotinEndocytosisPathology and Forensic Medicinechemistry.chemical_compoundmedicineCells CulturedPeroxidasebiologyCell CycleOryzaSerum Albumin BovineCell BiologyGeneral MedicineCell cyclePlant cellEndocytosisCell biologyNocodazolemedicine.anatomical_structureBiochemistrychemistrybiology.proteinIntracellularBiomarkersCell DivisionEuropean journal of cell biology
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Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer.

2004

Summary In mammals and yeast, a cytosolic dilysine motif is critical for endoplasmic reticulum (ER) localization of type I membrane proteins. Retrograde transport of type I membrane proteins containing dilysine motifs at their cytoplasmic carboxy (C)-terminal tail involves the interaction of these motifs with the COPI coat. The C-terminal dilysine motif has also been shown to confer ER localization to type I membrane proteins in plant cells. Using in vitro binding assays, we have analyzed sorting motifs in the cytosolic tail of membrane proteins, which may be involved in the interaction with components of the COPI coat in plant cells. We show that a dilysine motif in the −3,−4 position (rel…

CooperativityPlant ScienceBiologyCoatomer Proteinchemistry.chemical_compoundGeneticsAmino Acid SequencePlant ProteinsBinding SitesSequence Homology Amino AcidEndoplasmic reticulumProtoplastsMembrane ProteinsOryzaCell BiologyEndoplasmic reticulum localizationCOPIBrefeldin APeptide FragmentsCell biologyKineticsProtein SubunitsMembrane proteinchemistryAmino Acid SubstitutionCoatomerCytoplasmADP-Ribosylation Factor 1Sequence AlignmentSignal TransductionThe Plant journal : for cell and molecular biology
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