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van Anken, Eelco; Pena, Florentina; Hafkemeijer, Nicole; Christis, Chantal; Romijn, Edwin P; Grauschopf, Ulla; Oorschot, Viola M.J; Pertel, Thomas; Engels, Sander; Ora, Ari; Lástun, Viorica; Glockshuber, Rudi; Klumperman, Judith; Heck, Albert J.R; Luban, Jeremy; Braakman, Ineke
Proceedings of the National Academy of Sciences - PNAS, 10/2009, Letnik: 106, Številka: 40Journal Article
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)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.
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