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The Sep15 protein family: Roles in disulfide bond formation and quality control in the endoplasmic reticulum
Author(s) -
Labunskyy Vyacheslav M.,
Hatfield Dolph L.,
Gladyshev Vadim N.
Publication year - 2007
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540601126694
Subject(s) - endoplasmic reticulum , selenocysteine , protein disulfide isomerase , selenoprotein , microbiology and biotechnology , protein folding , biochemistry , disulfide bond , function (biology) , chemistry , secretory protein , secretory pathway , biology , enzyme , gene , cysteine , glutathione , glutathione peroxidase , golgi apparatus
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.IUBMB Life, 59: 1‐5, 2007