論文

査読有り
2013年9月10日

Stepwise Assembly of Fibrinogen Is Assisted by the Endoplasmic Reticulum Lectin-Chaperone System in HepG2 Cells

PLoS ONE
  • Taku Tamura
  • ,
  • Seisuke Arai
  • ,
  • Hisao Nagaya
  • ,
  • Jun Mizuguchi
  • ,
  • Ikuo Wada

8
9
開始ページ
e74580
終了ページ
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1371/journal.pone.0074580
出版者・発行元
9

The endoplasmic reticulum (ER) plays essential roles in protein folding and assembly of secretory proteins. ER-resident molecular chaperones and related enzymes assist in protein maturation by co-operated interactions and modifications. However, the folding/assembly of multimeric proteins is not well understood. Here, we show that the maturation of fibrinogen, a hexameric secretory protein (two trimers from α, β and γ subunits), occurs in a stepwise manner. The αγ complex, a precursor for the trimer, is retained in the ER by lectin-like chaperones, and the β subunit is incorporated into the αγ complex immediately after translation. ERp57, a protein disulfide isomerase homologue, is involved in the hexamer formation from two trimers. Our results indicate that the fibrinogen hexamer is formed sequentially, rather than simultaneously, using kinetic pause by lectin chaperones. This study provides a novel insight into the assembly of most abundant multi-subunit secretory proteins. © 2013 Tamura et al.

リンク情報
DOI
https://doi.org/10.1371/journal.pone.0074580
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/24040290

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