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| Subject Categories: Membranes & Transport | Proteins |
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| The EMBO Journal
(2008) 27, 315–327, doi:10.1038/sj.emboj.7601974 |
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| Protein quality control in the early secretory pathway |
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| Tiziana Anelli and Roberto Sitia |
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Department of Functional Genomics and Molecular Biology, Università Vita-Salute San Raffaele Scientific Institute, DiBiT-HSR, Milano, Italy To whom correspondence should be addressed Roberto Sitia, Department of Functional Genomics and Molecular Biology, Università Vita-Salute San Raffaele Scientific Institute, DiBiT-HSR, via Olgettina 58, Milan 20132, Italy. Tel.: +39 02 2643 4763; Fax: +39 02 2643 4723; E-mail: r.sitia@hsr.it Received 25 September 2007; Accepted 5 December 2007. |
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| Abstract |
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| 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. |
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| Keywords: endoplasmic reticulum, ER signalling, folding, protein degradation, protein secretion |
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