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Quantitative analysis of the human T cell palmitome
Palmitoylation is a reversible post-translational modification used to inducibly compartmentalize proteins in cellular membranes, affecting the function of receptors and intracellular signaling proteins. The identification of protein “palmitomes” in several cell lines raises the question to what ext...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4650600/ https://www.ncbi.nlm.nih.gov/pubmed/26111759 http://dx.doi.org/10.1038/srep11598 |
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author | Morrison, Eliot Kuropka, Benno Kliche, Stefanie Brügger, Britta Krause, Eberhard Freund, Christian |
author_facet | Morrison, Eliot Kuropka, Benno Kliche, Stefanie Brügger, Britta Krause, Eberhard Freund, Christian |
author_sort | Morrison, Eliot |
collection | PubMed |
description | Palmitoylation is a reversible post-translational modification used to inducibly compartmentalize proteins in cellular membranes, affecting the function of receptors and intracellular signaling proteins. The identification of protein “palmitomes” in several cell lines raises the question to what extent this modification is conserved in primary cells. Here we use primary T cells with acyl-biotin exchange and quantitative mass spectrometry to identify a pool of proteins previously unreported as palmitoylated in vivo. |
format | Online Article Text |
id | pubmed-4650600 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-46506002015-11-24 Quantitative analysis of the human T cell palmitome Morrison, Eliot Kuropka, Benno Kliche, Stefanie Brügger, Britta Krause, Eberhard Freund, Christian Sci Rep Article Palmitoylation is a reversible post-translational modification used to inducibly compartmentalize proteins in cellular membranes, affecting the function of receptors and intracellular signaling proteins. The identification of protein “palmitomes” in several cell lines raises the question to what extent this modification is conserved in primary cells. Here we use primary T cells with acyl-biotin exchange and quantitative mass spectrometry to identify a pool of proteins previously unreported as palmitoylated in vivo. Nature Publishing Group 2015-06-26 /pmc/articles/PMC4650600/ /pubmed/26111759 http://dx.doi.org/10.1038/srep11598 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Morrison, Eliot Kuropka, Benno Kliche, Stefanie Brügger, Britta Krause, Eberhard Freund, Christian Quantitative analysis of the human T cell palmitome |
title | Quantitative analysis of the human T cell palmitome |
title_full | Quantitative analysis of the human T cell palmitome |
title_fullStr | Quantitative analysis of the human T cell palmitome |
title_full_unstemmed | Quantitative analysis of the human T cell palmitome |
title_short | Quantitative analysis of the human T cell palmitome |
title_sort | quantitative analysis of the human t cell palmitome |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4650600/ https://www.ncbi.nlm.nih.gov/pubmed/26111759 http://dx.doi.org/10.1038/srep11598 |
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