2,977 research outputs found
Analysis of Cultured Human Melanocytes Based on Polymorphisms within the SLC45A2/MATP, SLC24A5/NCKX5, and OCA2/P Loci.
Reflections of a Jewish, Lesbian Author
In this essay, Jewish lesbian author Leslea Newman speaks of the importance of finding one's own identity reflected in works of literature, citing examples of her own work, and recommending the writings of other Jewish lesbian authors of merit
The Core Protein of the Basement-Membrane Heparan-Sulfate Proteoglycan (Bmhspg) Is Secreted Basally From Mdck Cells Treated with B-D-Xyloside
Distinct Coated Vesicles Labeled for P200 Bud From Trans-Golgi Network Membranes
Golgi-associated cytoplasmic proteins, such as the coatomer protein complex, are required for vesicle budding and trafficking. We have previously described a cytoplasmic phosphoprotein, p200, which binds dynamically and specifically to Golgi membranes. The p200 protein is dissociated from Golgi membranes in the presence of brefeldin A and it is induced to bind to Golgi membranes by activation of guanine nucleotide binding proteins (G proteins) with guanosine 5'-[gamma-thio] triphosphate or aluminum fluoride. To establish the role of p200 in vesicle budding, we localized membrane-bound p200 in intact cells and on isolated Golgi membranes. We show that p200 is preferentially associated with vesicles in the trans-Golgi network (TGN). Activation of G proteins induced budding and accumulation of small, coated vesicles from Golgi membranes and p200 was localized on the cytoplasmic surface of some of these resides. Using immunogold labeling we further demonstrate that p200 and beta-COP are localized on different populations of Golgi-derived vesicles. These data establish that p200 is involved in the budding and coating of a class of Golgi vesicles that are likely to be derived from the TGN. The data also show that there are distinct populations of non-clathrin-coated vesicles budded from Golgi membranes, and vesicles labeled for either beta-COP or p200 may represent transport vesicles for separate steps of protein transport
Moving Things Around - the Structural Basis of Intracellular Protein Trafficking - November 17-20, 1993 Chatham-Bars-Inn, Chatham, Ma
Protein trafficking and polarity in kidney epithelium: From cell biology to physiology
The transepithelial movement of fluids, electrolytes, and larger molecules is achieved by the activity of a host of specialized transporting proteins, including enzymes, receptors, and channels, that are located on either the apical, basal, or lateral plasma membrane domains of epithelial cells. In the kidney as well as in all other organs, this remarkable polarity of epithelial cells depends on the selective insertion of newly synthesized and recycling proteins and lipids into distinct plasma membrane domains and on the maintenance and modulation of these specialized domains once they are established during epithelial development, This review addresses the mechanisms by which epithelial cells control the movement of membrane components within the cell to ensure that they are delivered to the correct target membrane. Among the topics discussed are targeting signals within membrane proteins, the role of the cytoskeleton and the tight junctional barrier in cell polarity, and the requirement for accessory proteins in the targeting process, including GTP-binding proteins, and proteins that are involved in vesicle docking and fusion events. The final part of the review is devoted uniquely to the polarized targeting of functionally defined proteins in various kidney cell types. In concluding, examples of how a breakdown in these trafficking pathways may be related to some disease states are presented
Staging the life-world: Habermas and the recuperation of Austin speech act theory
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MODEIN2 and Colby: computer codes for sediment transport computations
November, 1976.CER76-77VMP-JL-DBS19
Tunneling microscopy of NbSe2 in air
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