Protein Disorder And Its Clinical Importance Essay

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Protein disorder in autophagy and its clinical importance: Autophagy is an intracellular reprocess route in eukaryotes whereby organelles and cytoplasm are sequestered in vesicles, which are subsequently release to the vacuole for breakdown. The process is build by various nutrient-responsive signaling cascades converging on the Autophagy-Related1 (ATG1)/ATG13 kinase complex. Synthesis of the ATG12-ATG5 and ATG8-phosphatidylethanolamine adducts, which are important for autophagy, still occurs in ATG13-deficient plants, but the biogenesis of ATG8-decorated autophagic bodies does not, showing that the complex regulates downstream events required for autophagosome enclosure and/or vacuolar delivery. Surprisingly, levels of the ATG1a and ATG13a phosphoproteins drop dramatically during nutrient starvation and rise again upon nutrient addition. This turnover is revoked by inhibition of the ATG system, indicating that the ATG1/13 complex becomes a target of autophagy. Consistent with this mechanism, ATG1a is supplied to the vacuole with ATG8-decorated autophagic bodies. Given its responsiveness to nutrient demands, the turnover of the ATG1/13 kinase likely gives a dynamic mechanism to tightly connect autophagy to a plant’s nutritional status. Eukaryotic cells can massively transfer their own cytoplasmic contents into a lytic compartment, the vacuole/lysosome, for reprocessing through a conserved system called autophagy. The key process in autophagy is the separation of cytoplasmic
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