Stepwise assembly of fibrinogen is assisted by the endoplasmic reticulum lectin-chaperone system in HepG2 cells.
Stepwise assembly of fibrinogen is assisted by the endoplasmic reticulum lectin-chaperone system in HepG2 cells.
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纤维蛋白原的逐步组装得到了HEPG2细胞中内质网凝集素 - 链酮系统的辅助组装。
DOI：
10.1371/journal.pone.0074580
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发表时间：
2013
期刊：
影响因子：
3.7
通讯作者：
Wada I
中科院分区：
文献类型：
--
作者：
Tamura T;Arai S;Nagaya H;Mizuguchi J;Wada I
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.
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