

Other version: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2761347/pdf/zpq17019.pdf
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Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1 |
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Authors | ![]() | |
Published in | Proceedings of the National Academy of Sciences of the United States of America. 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 Sequence — Animals — B-Lymphocytes/metabolism/ultrastructure — Cell Differentiation — Cell Line, Tumor — Electrophoresis, Gel, Two-Dimensional — Endoplasmic Reticulum/*metabolism — HeLa Cells — Heat-Shock Proteins/genetics/metabolism — Humans — Immunoblotting — Immunoglobulin M/*metabolism — Mass Spectrometry — Mice — Microscopy, Fluorescence — Microscopy, Immunoelectron — Molecular Chaperones/genetics/*metabolism — Oxidoreductases/metabolism — Plasma Cells/cytology/*metabolism — RNA Interference — Sulfhydryl Compounds/metabolism | |
Identifiers | PMID: 19805154 | |
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![]() ![]() Other version: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2761347/pdf/zpq17019.pdf |
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Structures | ||
Research group | Réplication virale, pathogénèse et immunité (848) | |
Citation (ISO format) | 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 of the United States of America, 2009, vol. 106, n° 40, p. 17019-17024. doi: 10.1073/pnas.0903036106 https://archive-ouverte.unige.ch/unige:20145 |