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lüll Secretory pathway quality control operating in Golgi, plasmalemmal, and endosomal systems Arvan P; Zhao X; Ramos-Castaneda J; Chang ATraffic 2002[Nov]; 3 (11): 771-80Exportable proteins that have significant defects in nascent polypeptide folding or subunit assembly are frequently retained in the endoplasmic reticulum and subject to endoplasmic reticulum-associated degradation by the ubiquitin-proteasome system. In addition to this, however, there is growing evidence for post-endoplasmic reticulum quality control mechanisms in which mutant or non-native exportable proteins may undergo anterograde transport to the Golgi complex and post-Golgi compartments before intracellular disposal. In some instances, these proteins may undergo retrograde transport back to the endoplasmic reticulum with re-targeting to the endoplasmic reticulum-associated degradation pathway; in other typical cases, they are targeted into the endosomal system for degradation by vacuolar/lysosomal proteases. Such quality control targeting is likely to involve recognition of features more commonly expressed in mutant proteins, but may also be expressed by wild-type proteins, especially in cells with perturbation of local environments that are essential for normal protein trafficking and stability in the secretory pathway and at the cell surface.|Animals[MESH]|Biological Transport[MESH]|Carrier Proteins/metabolism[MESH]|Cell Membrane/*metabolism[MESH]|Endoplasmic Reticulum/*metabolism[MESH]|Endosomes/*metabolism[MESH]|Golgi Apparatus/*metabolism[MESH]|Humans[MESH]|Membrane Proteins/metabolism[MESH]|Models, Biological[MESH]|Protein Transport[MESH] |