期刊
EMBO JOURNAL
卷 26, 期 19, 页码 4177-4188出版社
WILEY
DOI: 10.1038/sj.emboj.7601844
关键词
endoplasmic reticulum; ERGIC; IgM; protein folding; quality control
资金
- Telethon [GGP06155] Funding Source: Medline
The biogenesis of secretory IgM occurs stepwise under stringent quality control, formation of mu L-2(2) preceding polymerization. How is efficiency of IgM secretion coupled to fidelity? We show here that ERp44, a soluble protein involved in thiol-mediated retention, interacts with ERGIC-53. Binding to this hexameric lectin contributes to ERp44 localization in the ER-golgi intermediate compartment. ERp44 and ERGIC-53 increase during B-lymphocyte differentiation, concomitantly with the onset of IgM polymerization. Both preferentially bind mu L-2(2) and higher order intermediates. Their overexpression or silencing in non-lymphoid cells promotes or decreases secretion of IgM polymers, respectively. In IgM-secreting B-lymphoma cells, l chains interact first with BiP and later with ERp44 and ERGIC-53. Our findings suggest that ERGIC53 provides a platform that receives mu L-2(2) subunits from the BiP-dependent checkpoint, assisting polymerization. In this process, ERp44 couples thiol-dependent assembly and quality control.
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