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

van Anken, Eelco
Pena, Florentina
Hafkemeijer, Nicole
Christis, Chantal
Romijn, Edwin P.
Grauschopf, Ulla
Oorschot, Viola M. J.
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Published in Proceedings of the National Academy of Sciences. 2009, vol. 106, no. 40, p. 17019-17024
Abstract 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.
Keywords Amino Acid SequenceAnimalsB-Lymphocytes/metabolism/ultrastructureCell DifferentiationCell Line, TumorElectrophoresis, Gel, Two-DimensionalEndoplasmic Reticulum/*metabolismHeLa CellsHeat-Shock Proteins/genetics/metabolismHumansImmunoblottingImmunoglobulin M/*metabolismMass SpectrometryMiceMicroscopy, FluorescenceMicroscopy, ImmunoelectronMolecular Chaperones/genetics/*metabolismOxidoreductases/metabolismPlasma Cells/cytology/*metabolismRNA InterferenceSulfhydryl Compounds/metabolism
PMID: 19805154
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Research group Réplication virale, pathogénèse et immunité (848)
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VAN ANKEN, Eelco et al. Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1. In: Proceedings of the National Academy of Sciences, 2009, vol. 106, n° 40, p. 17019-17024. doi: 10.1073/pnas.0903036106 https://archive-ouverte.unige.ch/unige:20145

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Deposited on : 2012-04-23

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