Trans-Golgi network sorting
نویسندگان
چکیده
منابع مشابه
Lipid-dependent protein sorting at the trans-Golgi network.
In eukaryotic cells, the trans-Golgi network serves as a sorting station for post-Golgi traffic. In addition to coat- and adaptor-mediated mechanisms, studies in mammalian epithelial cells and yeast have provided evidence for lipid-dependent protein sorting as a major delivery mechanism for cargo sorting to the cell surface. The mechanism for lipid-mediated sorting is the generation of raft pla...
متن کاملThe trans-Golgi network: a late secretory sorting station.
Proteins synthesized on membrane-bound ribosomes are transported through the Golgi apparatus and, on reaching the trans-Golgi network, are sorted for delivery to various cellular destinations. Sorting involves the assembly of cytosol-oriented coat structures which preferentially package cargo into vesicular transport intermediates. Recent studies have shed new light on both the molecular machin...
متن کاملCompartmentation of the Golgi complex: brefeldin-A distinguishes trans- Golgi cisternae from the trans-Golgi network
The Golgi complex is composed of at least four distinct compartments, termed the cis-, medial, and trans-Golgi cisternae and the trans-Golgi network (TGN). It has recently been reported that the organization of the Golgi complex is disrupted in cells treated with the fungal metabolite, brefeldin-A. Under these conditions, it was shown that resident enzymes of the cis-, medial, and trans-Golgi r...
متن کاملFunctional characterization of protein-sorting machineries at the trans-Golgi network in Drosophila melanogaster.
Targeting of proteins to their final destination is a prerequisite for living cells to maintain their homeostasis. Clathrin functions as a coat that forms transport carriers called clathrin-coated vesicles (CCVs) at the plasma membrane and post-Golgi compartments. In this study, we established an experimental system using Schneider S2 cells derived from the fruit fly, Drosophila melanogaster, a...
متن کاملActin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network
Knockdown of the actin-severing protein actin-depolymerizing factor (ADF)/cofilin inhibited export of an exogenously expressed soluble secretory protein from Golgi membranes in Drosophila melanogaster and mammalian tissue culture cells. A stable isotope labeling by amino acids in cell culture mass spectrometry-based protein profiling revealed that a large number of endogenous secretory proteins...
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ژورنال
عنوان ژورنال: Cellular and Molecular Life Sciences
سال: 2001
ISSN: 1420-682X
DOI: 10.1007/pl00000922