Search results for "Coated Pits"

showing 2 items of 2 documents

Endocytosis in skeletal muscle fibers.

1999

Defining the organization of endocytic pathway in multinucleated skeletal myofibers is crucial to understand the routing of membrane proteins, such as receptors and glucose transporters, through this system. Here we analyzed the organization of the endocytic trafficking pathways in isolated rat myofibers. We found that sarcolemmal-coated pits and transferrin receptors were concentrated in the I band areas. Fluid phase markers were taken up into vesicles in the same areas along the whole length of the fibers and were then delivered into structures around and between the nuclei. These markers also accumulated beneath the neuromuscular and myotendinous junctions. The recycling compartment, lab…

Monosaccharide Transport ProteinsEndosomeEndocytic cycleMuscle Fibers SkeletalFluorescent Antibody TechniqueGene ExpressionMuscle ProteinsTransferrin receptorEndosomesBiologyEndocytosisMicrotubulesSarcolemmaMicrotubuleReceptors TransferrinMyocyteAnimalsMuscle SkeletalCells Culturedchemistry.chemical_classificationGlucose Transporter Type 4Cell MembraneCoated Pits Cell-MembraneCell BiologyEndocytosisCell biologyCell CompartmentationRatsMicroscopy ElectronMembrane proteinchemistryTransferrinLysosomesExperimental cell research
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Bradykinin-induced Internalization of the Human B2Receptor Requires Phosphorylation of Three Serine and Two Threonine Residues at Its Carboxyl Tail

1999

The binding of bradykinin (BK) to B2 receptor triggers the internalization of the agonist-receptor complex. To investigate the mechanisms and the receptor structures involved in this fundamental process of receptor regulation, the human B2 receptor was mutated within its cytoplasmic tail by complementary strategies of truncation, deletion, and amino acid substitution. Ligand binding, signal transduction, internalization as well as phosphorylation were studied for the mutated receptors expressed in COS, CHO, and HEK 293 cells. Truncation of 44 out of 55 amino acid residues of the receptor's cytoplasmic tail corresponding to positions 321-364 did not alter the kinetics of BK binding and the r…

ThreonineReceptor Bradykinin B2media_common.quotation_subjectMolecular Sequence DataCHO CellsBiologyBradykininTransfectionBiochemistryCell LineSerineCricetinaeSerineAnimalsHumans5-HT5A receptorAmino Acid SequencePhosphorylationInternalizationReceptorMolecular BiologyPeptide sequenceDNA Primersmedia_commonBase SequenceReceptors BradykininCoated Pits Cell-MembraneCell BiologyInterleukin-13 receptorClathrinEndocytosisRecombinant ProteinsCell biologyKineticsBiochemistryCOS CellsPhosphorylationSignal transductionJournal of Biological Chemistry
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