Protein quality control in the early secretory pathway.
Eukaryotic cells are able to discriminate between native and non-native polypeptides, selectively transporting the former to their final destinations. Secretory proteins are scrutinized at the endoplasmic reticulum (ER)-Golgi interface. Recent findings reveal novel features of the underlying molecular mechanisms, with several chaperone networks cooperating in assisting the maturation of complex proteins and being selectively induced to match changing synthetic demands. 'Public' and 'private' chaperones, some of which enriched in specializes subregions, operate for most or selected substrates, respectively. Moreover, sequential checkpoints are distributed along the early secretory pathway, allowing efficiency and fidelity in protein secretion.
Anelli
Tiziana
T
Department of Functional Genomics and Molecular Biology, Università Vita-Salute San Raffaele Scientific Institute, DiBiT-HSR, Milano, Italy.
Sitia
Roberto
R
D004721:Endoplasmic Reticulum / Q000378:metabolism*; D008954:Models, Biological; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction
D011506:Proteins