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

doi:10.1073/pnas.0903036106

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

IRCCS Ospedale San Raffaele

Research output: Contribution to journal › Article › peer-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 language	English
Pages (from-to)	17019-17024
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	106
Issue number	40
DOIs	https://doi.org/10.1073/pnas.0903036106
Publication status	Published - Oct 6 2009

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Van Anken, E., Pena, F., Hafkemeijer, N., Christis, C., Romijn, E. P., Grauschopf, U., Oorschot, V. M. J., Pertel, T., Engels, S., Ora, A., Lástun, V., Glockshuber, R., Klumperman, J., Heck, A. J. R., Luban, J., & Braakman, I. (2009). Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1. Proceedings of the National Academy of Sciences of the United States of America, 106(40), 17019-17024. https://doi.org/10.1073/pnas.0903036106

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; Pertel, Thomas; Engels, Sander; Ora, Ari; Lástun, Viorica; Glockshuber, Rudi; Klumperman, Judith; Heck, Albert J R; Luban, Jeremy; Braakman, Ineke.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 106, No. 40, 06.10.2009, p. 17019-17024.

Research output: Contribution to journal › Article › peer-review

Van Anken, E, Pena, F, Hafkemeijer, N, Christis, C, Romijn, EP, Grauschopf, U, Oorschot, VMJ, Pertel, T, Engels, S, Ora, A, Lástun, V, Glockshuber, R, Klumperman, J, Heck, AJR, Luban, J & Braakman, I 2009, 'Efficient IgM assembly and secretion require the plasma cell induced endoplasmic reticulum protein pERp1', Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 40, pp. 17019-17024. https://doi.org/10.1073/pnas.0903036106

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. / 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, No. 40. pp. 17019-17024.

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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.",

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AU - Romijn, Edwin P.

AU - Grauschopf, Ulla

AU - Oorschot, Viola M J

AU - Pertel, Thomas

AU - Engels, Sander

AU - Ora, Ari

AU - Lástun, Viorica

AU - Glockshuber, Rudi

AU - Klumperman, Judith

AU - Heck, Albert J R

AU - Luban, Jeremy

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AB - 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.

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

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