Stepwise Assembly of Fibrinogen Is Assisted by the Endoplasmic Reticulum Lectin-Chaperone System in HepG2 Cells
説明
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 a, b and c subunits), occurs in a stepwise manner. The ac complex, a precursor for the trimer, is retained in the ER by lectin-like chaperones, and the b subunit is incorporated into the ac 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.
収録刊行物
-
- PLoS ONE
-
PLoS ONE 8 (9), e74580-, 2013
PLoS
- Tweet
詳細情報 詳細情報について
-
- CRID
- 1050571704604472832
-
- NII論文ID
- 120007172098
-
- HANDLE
- 10295/00005834
-
- 本文言語コード
- en
-
- 資料種別
- journal article
-
- データソース種別
-
- IRDB
- CiNii Articles