エンドウ トシヤ   ENDO TOSHIYA
  遠藤 斗志也
   所属   京都産業大学  生命科学部 先端生命科学科
   職種   客員教授
言語種別 英語
発行・発表の年月 2009/05
形態種別 研究論文
査読 査読あり
標題 Roles of Protein-disulfide Isomerase-mediated Disulfide Bond Formation of Yeast Mnl1p in Endoplasmic Reticulum-associated Degradation
執筆形態 その他
掲載誌名 JOURNAL OF BIOLOGICAL CHEMISTRY
出版社・発行元 AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
巻・号・頁 284(18),pp.11815-11825
著者・共著者 Machiko Sakoh-Nakatogawa,Shuh-ichi Nishikawa,Toshiya Endo
概要 The endoplasmic reticulum (ER) has a strict protein quality control system. Misfolded proteins generated in the ER are degraded by the ER-associated degradation (ERAD). Yeast Mnl1p consists of an N-terminal mannosidase homology domain and a less conserved C-terminal domain and facilitates the ERAD of glycoproteins. We found that Mnl1p is an ER luminal protein with a cleavable signal sequence and stably interacts with a protein-disulfide isomerase (PDI). Analyses of a series of Mnl1p mutants revealed that interactions between the C-terminal domain of Mnl1p and PDI, which include an intermolecular disulfide bond, are essential for subsequent introduction of a disulfide bond into the mannosidase homology domain of Mnl1p by PDI. This disulfide bond is essential for the ERAD activity of Mnl1p and in turn stabilizes the prolonged association of PDI with Mnl1p. Close interdependence between Mnl1p and PDI suggests that these two proteins form a functional unit in the ERAD pathway.
DOI 10.1074/jbc.M900813200
ISSN 0021-9258
PMID 19279007