4.8 Article

Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1

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NATL ACAD SCIENCES
DOI: 10.1073/pnas.0903036106

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  1. EuroSCOPE
  2. Zon-MW
  3. NWO-CW
  4. The Netherlands Proteomics Centre
  5. Swiss National Science Foundation
  6. National Institute of Allergy and Infectious Diseases
  7. Sigrid Juselius Foundation

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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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