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Summary
The cellular proteome is maintained by a dynamic balance between protein synthesis and degradation, known as proteostasis. An imperative of successful proteostasis is the detection and removal of misfolded proteins by quality control pathways. Proteins that result from translation errors, misfolding, or age-induced or chemical damage, as well as orphan proteins (which result from inappropriate stoichiometry of multiprotein complexes), are all subject to a variety of degradative pathways to limit their cellular accumulation, which can be toxic (1). One of the striking features of degradative quality control is the juxtaposition of high specificity for misfolded versions of normal proteins with the very broad range of substrates that can be accommodated by each pathway. On pages 472 and 471 of this issue, Yanagitani et al. (2) and Nguyen et al. (3), respectively, show that a newly discovered quality control pathway is used to bring about the sweeping changes in proteome content that are observed in the differentiation of relatively “cellular” reticulocytes to the highly specialized hemoglobin-rich red blood cells (erythrocytes) (4, 5).
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