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*

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

45 Citations (Scopus)

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 - 6 Oct 2009
MoE publication typeA1 Journal article-refereed

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