Clathrin
Mostrando 1-12 de 466 artigos, teses e dissertações.
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1. Estudo in vitro sobre a interação celular e vias endocíticas de papilomavírus humano (HPV) em leucócitos do sangue periférico. / In vitro study on the interaction of human papillomavirus in cell from peripheral blood leukocytes.
Human papillomavirus (HPV) is the primary etiologic agent of anogenital and cervical cancer, caused mainly by the high-risk HPV16 and HPV18 viruses. Recent studies revealed that besides the sexual transmission of HPV, there are other forms of contagion. However, the difficulty in obtaining quantities of viable wild-type or mutant of HPV constitutes a limitin
Publicado em: 2009
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2. Expression of USP2a and study of its interaction with clathrin in human oral squamous carcinoma and prostate cancer cells / Estudo da expressão da enzima desubiquitinante USP2a e de sua interação com a proteina clatrina em celulas derivadas de carcinomas espinocelulares bucais e de prostata humanos
The ubiquitin (Ub)-proteasome pathway controls cellular protein turnover by degrading targeted intracellular proteins tagged with poly-Ub chains. Ubiquitination is a reversible process and the deubiquitinating enzymes (DUBs) are proteases that specifically cleave off Ub from Ub-protein conjugates. They can act in a preproteasomal level removing the poly-Ub t
Publicado em: 2007
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3. Trypanosoma cruzi: Contribuição ao estudo da endocitose dependente e independente de clatrina em formas epimastigotas. / Trypanosoma cruzi: Contribution to the study of the dependent and independent endocytosis of clatrina in epimastigote forms.
Endocitose em células eucarióticas é o processo de incorporação de macromoléculas por diferentes vias, com diversas proteínas associadas. Este processo ocorre através do brotamento de vesículas na membrana plasmática e endereçamento destas vesículas a compartimentos endossomais no citoplasma. Os tripanossomatídeos são protozoários flagelados p
Publicado em: 2007
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4. Sinais de tráfego envolvidos no envolvidos no endereçamento do transportador vesicular de acetilcolina (VAChT)
The vesicular acetylcholine transporter (VAChT) is the protein responsible for packaging cytoplasmic acetylcholine (ACh) into the synaptic vesicle of cholinergic neurons. The cytosolic C-terminal region of VAChT is important in intracellular trafficking events and targeting to secretory organelles. In this study, we evaluate the existence of trafficking sign
Publicado em: 2006
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5. Internalização e tráfego da Stress Inducible Protein-1 (STI-1), um ligante da proteína prion celular
The cellular prion protein (PrPc) is a glycosylphosphatidylinositol (GPI)-anchored plasma membrane glycoprotein. The PrPc abnormal isoform, PrPsc, is an infectious form involved in the prion disease pathogenesis. Identification of ligands that interact with PrPc can help in the understanding the physiological function of this protein. The STI-1 (stress induc
Publicado em: 2006
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6. Adaptor and Clathrin Exchange at the Plasma Membrane and trans-Golgi Network
We previously demonstrated, using fluorescence recovery after photobleaching, that clathrin in clathrin-coated pits at the plasma membrane exchanges with free clathrin in the cytosol, suggesting that clathrin-coated pits are dynamic structures. We now investigated whether clathrin at the trans-Golgi network as well as the clathrin adaptors AP2 and AP1 in cla
The American Society for Cell Biology.
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7. Spatially Regulated Recruitment of Clathrin to the Plasma Membrane during Capping and Cell TranslocationV⃞
Clathrin-coated vesicles bud from selected cellular membranes to traffic-specific intracellular proteins. To study the dynamic properties of clathrin-coated membranes, we expressed clathrin heavy chain tagged with green fluorescent protein (GFP) in Dictyostelium cells. GFP-clathrin was functional and retained the native properties of clathrin: the chimeric p
The American Society for Cell Biology.
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8. Clathrin Assembly Lymphoid Myeloid Leukemia (CALM) Protein: Localization in Endocytic-coated Pits, Interactions with Clathrin, and the Impact of Overexpression on Clathrin-mediated Traffic
The clathrin assembly lymphoid myeloid leukemia (CALM) gene encodes a putative homologue of the clathrin assembly synaptic protein AP180. Hence the biochemical properties, the subcellular localization, and the role in endocytosis of a CALM protein were studied. In vitro binding and coimmunoprecipitation demonstrated that the clathrin heavy chain is the major
The American Society for Cell Biology.
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9. γ Subunit of the AP-1 Adaptor Complex Binds Clathrin: Implications for Cooperative Binding in Coated Vesicle Assembly
The heterotetrameric AP-1 adaptor complex is involved in the assembly of clathrin-coated vesicles originating from the trans-Golgi network (TGN). The β1 subunit of AP-1 is known to contain a consensus clathrin binding sequence, LLNLD (the so-called clathrin box motif), in its hinge segment through which the β chain interacts with the N-terminal domain
The American Society for Cell Biology.
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10. Adaptor Complex-independent Clathrin Function in Yeast
Clathrin-associated adaptor protein (AP) complexes are major structural components of clathrin-coated vesicles, functioning in clathrin coat assembly and cargo selection. We have carried out a systematic biochemical and genetic characterization of AP complexes in Saccharomyces cerevisiae. Using coimmunoprecipitation, the subunit composition of two complexes,
The American Society for Cell Biology.
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11. Clathrin-independent endocytosis of ubiquitinated cargos
Plasma membrane receptors can be endocytosed through clathrin-dependent and clathrin-independent pathways. Here, we show that the epidermal growth factor (EGF) receptor (EGFR), when stimulated with low doses of EGF, is internalized almost exclusively through the clathrin pathway, and it is not ubiquitinated. At higher concentrations of ligand, however, a sub
National Academy of Sciences.
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12. Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking*
Non-visual arrestins play a pivotal role as adaptor proteins in regulating the signaling and trafficking of multiple classes of receptors. Although arrestin interaction with clathrin, AP-2, and phosphoinositides contributes to receptor trafficking, little is known about the configuration and dynamics of these interactions. Here, we identify a novel interface
American Society for Biochemistry and Molecular Biology.