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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...

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Autores principales: Morrison, Eliot, Kuropka, Benno, Kliche, Stefanie, Brügger, Britta, Krause, Eberhard, Freund, Christian
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
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.
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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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