Journal
IUBMB LIFE
Volume 59, Issue 1, Pages 1-5Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15216540601126694
Keywords
selenoprotein; disulfide bond formation; endoplasmic reticulum; protein folding; thiol-disulfide oxidoreductase
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Funding
- Intramural NIH HHS Funding Source: Medline
- NCI NIH HHS [CA 080946] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [Z01BC005317, R01CA080946] Funding Source: NIH RePORTER
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Disulfide bonds play an important role in the structure and function of membrane and secretory proteins. The formation of disulfide bonds in the endoplasmic reticulum ( ER) of eukaryotic cells is catalyzed by a complex network of thiol-disulfide oxidoreductases. Whereas a number of ER-resident oxidoreductases have been identified, the function of only a few of them is firmly established. Recently, a selenocysteine-containing oxidoreductase, Sep15, has been implicated in disulfide bond assisted protein folding, and a role in quality control for this selenoprotein has been proposed. This review summarizes up-to-date information on the Sep15 family proteins and highlights new insights into their physiological function.
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