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Protein turnover: to self-eat or not to self-eat, that’s the question.
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Noushin Nabavi
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University of California, San Francisco
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Department of Cellular and Molecular Pharmacology. UCSF, San Francisco 94107, USA.
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noushin.nabavi@ucsf.edu
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The regulated balance between protein synthesis and protein degradation is crucial for tissue integrity, homeostasis, and maintenance. There are two principal routes for intracellular protein degradation, namely the ubiquitin proteasome system (UPS) and the autophagy-lysosome pathway (ALP) (Alfred 2003; Martinez-Vicente, Sovak et al. 2005). There are also emerging evidences for the interaction of the two pathways through specific molecular chaperones that can assist in recognizing, tethering, and degrading misfolded or aggregated protein substrates. Any misfolded or aggregated protein needs to be immediately cleared through either or both degradation pathways since the failure to do so can lead to cytotoxic stress due to accumulation of unwanted protein substrates. This stress can then lead to pathogenesis and tumorigenesis. In fact, most age-related diseases and cancers are characterized by a deregulation in either the UPS or ALP machineries. In this review, I intend to analyze the recent findings of cellular and molecular moieties in the autophagic degradation pathway, how this pathway is studied, and how it pertains to disease.
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