| Title | Sec61p is required for ERAD-L: genetic dissection of the translocation and ERAD-L functions of Sec61p using novel derivatives of CPY. | | Author(s) | Willer M, Forte GM, Stirling CJ | | Institution | Faculty of Life Sciences, University of Manchester, Manchester M13 9PT. | | Source | J Biol Chem 2008 Sep 25. | | Abstract | Misfolded proteins in the endoplasmic reticulum (ER) are exported to the cytosol for degradation by the proteasome in a process known as ER-associated degradation (ERAD). CPY* is a well characterised ERAD substrate whose degradation is dependent upon the Hrd1-complex. However, while the functions of some of the components of this complex are known, the nature of the protein dislocation channel remains obscure. Sec61p has been suggested as an obvious candidate due to its role as a protein conducting channel through which polypeptides are initially translocated into the ER. However, it has not yet been possible to functionally dissect any role for Sec61p in dislocation from its essential function in translocation. By changing the translocation properties of a series of novel ERAD substrates we are able to separate these two events and find that functional Sec61p is essential for the ERAD-L pathway. | | Language | ENG | | Pub Type(s) | JOURNAL ARTICLE
| | PubMed ID | 18819915 |
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