Anelli Tiziana, Sitia Roberto
Department of Functional Genomics and Molecular Biology, Università Vita-Salute San Raffaele Scientific Institute, DiBiT-HSR, Milano, Italy.
EMBO J. 2008 Jan 23;27(2):315-27. doi: 10.1038/sj.emboj.7601974.
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.
真核细胞能够区分天然和非天然多肽,选择性地将前者运输到其最终目的地。分泌蛋白在内质网(ER)-高尔基体界面受到严格审查。最近的研究结果揭示了潜在分子机制的新特征,几个伴侣蛋白网络协同作用,协助复杂蛋白质的成熟,并被选择性诱导以适应不断变化的合成需求。“公共”和“私人”伴侣蛋白,其中一些富集于特定亚区域,分别作用于大多数或选定的底物。此外,连续的检查点分布在早期分泌途径中,确保蛋白质分泌的效率和保真度。