کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2048531 | 1074083 | 2011 | 6 صفحه PDF | دانلود رایگان |
Misfolded, luminal endoplasmic reticulum (ER) proteins must be recognized before being degraded by a process called ERAD-L. Using site-specific photocrosslinking in Saccharomyces cerevisiae, we tested luminal interactions of a glycosylated ERAD-L substrate with potential recognition components. Major interactions were observed with Hrd3p. These are independent of the glycan and of other ERAD components, and can occur throughout the length of the unfolded substrate. The lectin Yos9p only interacts with a polypeptide segment distant from the degradation signal. Hrd3p may thus be the first substrate-recognizing component. Der1p appears to have a role in a pathway that is parallel to that involving Hrd3p.Structured summary of protein interactionssCPYphysically interacts with sCPY by cross-linking study (View interaction)Hrd3 and sCPYphysically interact by cross-linking study (View interaction)
Journal: FEBS Letters - Volume 585, Issue 9, 6 May 2011, Pages 1281–1286