期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 106, 期 40, 页码 17019-17024出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0903036106
关键词
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资金
- EuroSCOPE
- Zon-MW
- NWO-CW
- The Netherlands Proteomics Centre
- Swiss National Science Foundation
- National Institute of Allergy and Infectious Diseases
- Sigrid Juselius Foundation
Plasma cells daily secrete their own mass in antibodies, which fold and assemble in the endoplasmic reticulum ( ER). To reach these levels, cells require pERp1, a novel lymphocyte-specific small ER-resident protein, which attains expression levels as high as BiP when B cells differentiate into plasma cells. Although pERp1 has no homology with known ER proteins, it does contain a CXXC motif typical for oxidoreductases. In steady state, the CXXC cysteines are locked by two parallel disulfide bonds with a downstream C(X)(6)C motif, and pERp1 displays only modest oxidoreductase activity. pERp1 emerged as a dedicated folding factor for IgM, associating with both heavy and light chains and promoting assembly and secretion of mature IgM.
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