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

Eelco Van Anken, Florentina Pena, Nicole Hafkemeijer, Chantal Christis, Edwin P. Romijn, Ulla Grauschopf, Viola M J Oorschot, Thomas Pertel, Sander Engels, Ari Ora, Viorica Lástun, Rudi Glockshuber, Judith Klumperman, Albert J R Heck, Jeremy Luban, Ineke Braakman

Research output: Contribution to journalArticlepeer-review

Abstract

Plasma cells daily secrete theirownmass 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)6C 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.

Original languageEnglish
Pages (from-to)17019-17024
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume106
Issue number40
DOIs
Publication statusPublished - Oct 6 2009

ASJC Scopus subject areas

  • General

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