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Protein S-palmitoylation in cellular differentiation
Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein–protein and membrane–protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an importa...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Portland Press Ltd.
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5310721/ https://www.ncbi.nlm.nih.gov/pubmed/28202682 http://dx.doi.org/10.1042/BST20160236 |
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author | Zhang, Mingzi M. Hang, Howard C. |
author_facet | Zhang, Mingzi M. Hang, Howard C. |
author_sort | Zhang, Mingzi M. |
collection | PubMed |
description | Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein–protein and membrane–protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate diverse biological processes as cells transition from one state to another. Here, we review the strategies and tools to analyze in vivo protein palmitoylation and interrogate the functions of the enzymes that put on and take off palmitate from proteins. We also highlight palmitoyl proteins and palmitoylation-related enzymes that are associated with cellular differentiation and/or tissue development in yeasts, protozoa, mammals, plants and other model eukaryotes. |
format | Online Article Text |
id | pubmed-5310721 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Portland Press Ltd. |
record_format | MEDLINE/PubMed |
spelling | pubmed-53107212017-02-27 Protein S-palmitoylation in cellular differentiation Zhang, Mingzi M. Hang, Howard C. Biochem Soc Trans Review Articles Reversible protein S-palmitoylation confers spatiotemporal control of protein function by modulating protein stability, trafficking and activity, as well as protein–protein and membrane–protein associations. Enabled by technological advances, global studies revealed S-palmitoylation to be an important and pervasive posttranslational modification in eukaryotes with the potential to coordinate diverse biological processes as cells transition from one state to another. Here, we review the strategies and tools to analyze in vivo protein palmitoylation and interrogate the functions of the enzymes that put on and take off palmitate from proteins. We also highlight palmitoyl proteins and palmitoylation-related enzymes that are associated with cellular differentiation and/or tissue development in yeasts, protozoa, mammals, plants and other model eukaryotes. Portland Press Ltd. 2017-02-08 2017-02-15 /pmc/articles/PMC5310721/ /pubmed/28202682 http://dx.doi.org/10.1042/BST20160236 Text en © 2017 The Author(s) https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-ND) (https://creativecommons.org/licenses/by-nc-nd/4.0/) . |
spellingShingle | Review Articles Zhang, Mingzi M. Hang, Howard C. Protein S-palmitoylation in cellular differentiation |
title | Protein S-palmitoylation in cellular differentiation |
title_full | Protein S-palmitoylation in cellular differentiation |
title_fullStr | Protein S-palmitoylation in cellular differentiation |
title_full_unstemmed | Protein S-palmitoylation in cellular differentiation |
title_short | Protein S-palmitoylation in cellular differentiation |
title_sort | protein s-palmitoylation in cellular differentiation |
topic | Review Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5310721/ https://www.ncbi.nlm.nih.gov/pubmed/28202682 http://dx.doi.org/10.1042/BST20160236 |
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