Search results for "Coat Protein Complex I"

showing 3 items of 3 documents

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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Retention mechanisms for ER and Golgi membrane proteins

2014

Unless there are mechanisms to selectively retain membrane proteins in the endoplasmic reticulum (ER) or in the Golgi apparatus, they automatically proceed downstream to the plasma or vacuole membranes. Two types of coat protein complex I (COPI)-interacting motifs in the cytosolic tails of membrane proteins seem to facilitate membrane retention in the early secretory pathway of plants: a dilysine (KKXX) motif (which is typical of p24 proteins) for the ER and a KXE/D motif (which occurs in the Arabidopsis endomembrane protein EMP12) for the Golgi apparatus. The KXE/D motif is highly conserved in all eukaryotic EMPs and is additionally present in hundreds of other proteins of unknown subcellu…

Golgi membraneSecretory PathwayKKXXMolecular Sequence DataGolgi ApparatusMembrane ProteinsGolgi TargetingPlant ScienceCOPIGolgi apparatusBiologyEndoplasmic ReticulumCoat Protein Complex ICell biologysymbols.namesakeMembrane proteinPlant CellssymbolsAmino Acid SequenceIntegral membrane proteinSecretory pathwayTrends in Plant Science
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Arabidopsis p24δ5 and p24δ9 facilitate Coat Protein I-dependent transport of the K/HDEL receptor ERD2 from the Golgi to the endoplasmic reticulum.

2014

The p24 proteins belong to a family of type I membrane proteins which cycle between the endoplasmic reticulum (ER) and Golgi via coat protein I (COPI) and COPII vesicles. Current nomenclature classifies them into four subfamilies, although plant p24 proteins belong to either the p24β or the p24δ subfamilies. Here, we show that Arabidopsis p24δ5/δ9 and HDEL ligands shift the steady-state distribution of the K/HDEL receptor ERD2 from the Golgi to the ER. We also show that p24δ5/δ9 interact directly with ERD2. This interaction requires the Golgi dynamics (GOLD) domain in p24δ5 and is much higher at acidic than at neutral pH, consistent with both proteins interacting at the cis-Golgi. In additi…

Receptors PeptideArabidopsisGolgi ApparatusPlant ScienceBiologyEndoplasmic ReticulumCoat Protein Complex Isymbols.namesakeGeneticsAnimalsSecretionCOPIIVesicular-tubular clusterArabidopsis ProteinsEndoplasmic reticulumMembrane ProteinsCell BiologyCOPIGolgi apparatusCell biologyTransport proteinDNA-Binding ProteinsProtein TransportMembrane proteinsymbolsTranscription FactorsThe Plant journal : for cell and molecular biology
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