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Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23
S-palmitoylation is a reversible post-translational modification important for controlling the membrane targeting and function of numerous membrane proteins with diverse roles in signalling, scaffolding, and trafficking. We sought to identify novel palmitoylated proteins in B lymphocytes using acyl-...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355122/ https://www.ncbi.nlm.nih.gov/pubmed/22615937 http://dx.doi.org/10.1371/journal.pone.0037187 |
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author | Ivaldi, Corinne Martin, Brent R. Kieffer-Jaquinod, Sylvie Chapel, Agnès Levade, Thierry Garin, Jérôme Journet, Agnès |
author_facet | Ivaldi, Corinne Martin, Brent R. Kieffer-Jaquinod, Sylvie Chapel, Agnès Levade, Thierry Garin, Jérôme Journet, Agnès |
author_sort | Ivaldi, Corinne |
collection | PubMed |
description | S-palmitoylation is a reversible post-translational modification important for controlling the membrane targeting and function of numerous membrane proteins with diverse roles in signalling, scaffolding, and trafficking. We sought to identify novel palmitoylated proteins in B lymphocytes using acyl-biotin exchange chemistry, coupled with differential analysis by liquid-chromatography tandem mass spectrometry. In total, we identified 57 novel palmitoylated protein candidates from human EBV-transformed lymphoid cells. Two of them, namely CD20 and CD23 (low affinity immunoglobulin epsilon Fc receptor), are immune regulators that are effective/potential therapeutic targets for haematological malignancies, autoimmune diseases and allergic disorders. Palmitoylation of CD20 and CD23 was confirmed by heterologous expression of alanine mutants coupled with bioorthogonal metabolic labeling. This study demonstrates a new subset of palmitoylated proteins in B cells, illustrating the ubiquitous role of protein palmitoylation in immune regulation. |
format | Online Article Text |
id | pubmed-3355122 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33551222012-05-21 Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 Ivaldi, Corinne Martin, Brent R. Kieffer-Jaquinod, Sylvie Chapel, Agnès Levade, Thierry Garin, Jérôme Journet, Agnès PLoS One Research Article S-palmitoylation is a reversible post-translational modification important for controlling the membrane targeting and function of numerous membrane proteins with diverse roles in signalling, scaffolding, and trafficking. We sought to identify novel palmitoylated proteins in B lymphocytes using acyl-biotin exchange chemistry, coupled with differential analysis by liquid-chromatography tandem mass spectrometry. In total, we identified 57 novel palmitoylated protein candidates from human EBV-transformed lymphoid cells. Two of them, namely CD20 and CD23 (low affinity immunoglobulin epsilon Fc receptor), are immune regulators that are effective/potential therapeutic targets for haematological malignancies, autoimmune diseases and allergic disorders. Palmitoylation of CD20 and CD23 was confirmed by heterologous expression of alanine mutants coupled with bioorthogonal metabolic labeling. This study demonstrates a new subset of palmitoylated proteins in B cells, illustrating the ubiquitous role of protein palmitoylation in immune regulation. Public Library of Science 2012-05-17 /pmc/articles/PMC3355122/ /pubmed/22615937 http://dx.doi.org/10.1371/journal.pone.0037187 Text en Ivaldi et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Ivaldi, Corinne Martin, Brent R. Kieffer-Jaquinod, Sylvie Chapel, Agnès Levade, Thierry Garin, Jérôme Journet, Agnès Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title | Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title_full | Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title_fullStr | Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title_full_unstemmed | Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title_short | Proteomic Analysis of S-Acylated Proteins in Human B Cells Reveals Palmitoylation of the Immune Regulators CD20 and CD23 |
title_sort | proteomic analysis of s-acylated proteins in human b cells reveals palmitoylation of the immune regulators cd20 and cd23 |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3355122/ https://www.ncbi.nlm.nih.gov/pubmed/22615937 http://dx.doi.org/10.1371/journal.pone.0037187 |
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