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Insulin Biosynthesis, Secretion, and Action | …
Polarized cells such as epithelia maintain distinct apical and basolateral plasma membrane domains with distinct protein and lipid compositions. These specializations of the plasma membrane require complex membrane trafficking pathways thought to include unique basolateral versus apical sorting mechanisms in the secretory pathway to direct newly synthesized proteins to the correct membrane domain. Additional regulation of the endocytosis pathway maintains polarity of lipid and protein components after internalization and recycling.
We demonstrate that arylomycin activity is conserved against a broad range of Y. pestis strains and that this activity results from SPase inhibition. The origins of the sensitivity are traced to an increased dependence on SPase that results from high levels of protein secretion under physiological conditions.
Insulin is produced in the beta cells of the pancreatic islets
As in other eukaryotes cells possess an endoplasmic reticulum into which most membrane or secretory proteins are inserted co-translationally. Some lumenal ER-resident proteins are retained in the ER by KDEL or HDEL signals in their extreme C-termini. cells also possess Golgi stacks, the next organelle through which secretory proteins pass. Unlike mammalian cells, invertebrates such as have many small "mini stacks" throughout the cytoplasm of most cells rather than one large stack positioned near the nucleus. From the Golgi, secretory proteins and some membrane proteins proceed to either the plasma membrane or to the endosomal system, depending upon various signals embedded in the primary sequence of the proteins. does not possess any obvious homologs of the mannose-6-phosphate receptors, and so may not use the mannose-6-phosphate system for tagging and sorting newly synthesized lysosomal hydrolases. Worms may instead use amino acid based signals and a vps10/sortillin receptor type system for such sorting, as is known to be the case in yeast.
Figure 4. GFP endocytosis by coelomocytes. Signal sequence-tagged GFP is synthesized in muscle and secreted into the body cavity. Coelomocytes efficiently take up GFP from the body cavity and accumulate GFP in large vesicles. Fluorescent micrograph of wild-type and typical mutant worms expressing GFP are shown. High magnification image of a wild-type coelomocyte is also shown.
Unfolded protein response - Wikipedia
We review the information gained from the use of SPase inhibitors as probes of prokaryote biology. A thorough understanding of the consequences of SPase inhibition and the mechanisms of resistance that arise are essential to the success of SPase as an antibiotic target. In addition to the role of SPase in processing secreted proteins, the use of SPase inhibitors has elucidated a previously unknown function for SPase in regulating cleavage events of membrane proteins.
This work describes the use of an arylomycin derivative, along with two-dimensional gel electrophoresis and LC-MS/MS, to identify eleven proteins whose secretion from stationary phase S. epidermidis is dependent on SPase activity. The data also suggest that the arylomycins should be valuable chemical biology tools for the study of protein secretion in a wide variety of different bacteria.
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Protein Synthesis -Translation and Regulation
Figure 3. YP170::GFP endocytosis by oocytes. YP170::GFP is synthesized in the intestine and secreted into the body cavity from which it is endocytosed by oocytes. is the yolk receptor expressed in oocytes. Fluorescent micrographs of wild-type and typical mutant worms expressing YP170::GFP are shown.
Difficult to Express Proteins - Protein Engineering Summit
One important model for mechanistic studies of endocytosis in focuses on oocytes, which internalize huge quantities of yolk proteins and their associated lipids by clathrin-mediated endocytosis (). This process is most easily followed by fluorescence microscopy using strains that express transgenes encoding the major yolk protein YP-170 (aka ) fused to GFP (; ). YP170-GFP is synthesized in the intestine of adult hermaphrodites and is secreted basolaterally into the body cavity (pseudocoelom). YP170-GFP, like endogenous yolk, is a cholesterol binding/transport protein related to human ApoB-100, the major protein component of serum low-density lipoprotein (LDL). The yolk receptor in is , an LDL-receptor related molecule expressed specifically in the oocytes (; ). contains a typical NPXY internalization motif in its intracellular domain that is known to direct other members of the LDL-receptor family into clathrin-coated pits. Trafficking of yolk and yolk receptors also depends critically upon the activities of the endocytic Rab proteins , , and , known modulators of endocytosis in all eukaryotes (). Thus yolk uptake provides a genetically tractable system for the study of clathrin and Rab dependent transport processes.
Vitamin B3 (Niacin) - Scientific Review on Usage, …
Screens for mutants defective in YP170-GFP uptake by oocytes identified 11 genes (eceptor-ediated ndocytosis defective) required for various steps in endocytic transport (; ). In contrast to secretory defects, defects in endocytosis do not severely affect the organization or morphology of the germ line or oocytes as judged by Nomarski optics. The best studied of the general endocytosis regulators identified in this screen are and (; ). Both of these proteins are found in the cytoplasm of most cells and are associated with the limiting membrane of endosomes. is an EH domain protein associated with recycling endosomes and is thought to contribute to the formation of membrane tubules that recycle receptors from endosomes to the cell surface (). There are several mammalian homologues of , at least one of which functions in recycling endosomes (). In the absence of , yolk receptors become trapped in endosomes of the oocyte and cannot efficiently recycle through multiple rounds of endocytosis. mutants are also defective in endocytosis by coelomocytes and in basolateral endocytic traffic in the intestine ().
Basic Immunology - Functions and disorders of the …
A simpler and more generally useful assay for coelomocyte endocytic function was developed by Fares and Greenwald (; ; ). They created transgenic worms expressing signal sequence-GFP fusion protein in body-wall muscles (p). In this strain, GFP is constitutively secreted from body-wall muscle cells into the pseudocoelom and is then efficiently taken up and degraded by coelomocytes. At steady-state this strain shows weak pseudocoelom labeling and stronger labeling of late endosome and lysosome structures within coelomocytes. Using this assay, (oelomocyte take defective) mutants were identified that show accumulation of GFP in the pseudocoelom, and/or aberrant morphology of endocytic organelles within coelomocytes (; ).
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