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MS‐based strategies for identification of protein SUMOylation modification
Protein SUMOylation modification conjugated with small ubiquitin‐like modifiers (SUMOs) is one kind of PTMs, which exerts comprehensive roles in cellular functions, including gene expression regulation, DNA repair, intracellular transport, stress responses, and tumorigenesis. With the development of...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899701/ https://www.ncbi.nlm.nih.gov/pubmed/31216068 http://dx.doi.org/10.1002/elps.201900100 |
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author | Sheng, Zenghua Wang, Xixi Ma, Yanni Zhang, Dan Yang, Yanfang Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang |
author_facet | Sheng, Zenghua Wang, Xixi Ma, Yanni Zhang, Dan Yang, Yanfang Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang |
author_sort | Sheng, Zenghua |
collection | PubMed |
description | Protein SUMOylation modification conjugated with small ubiquitin‐like modifiers (SUMOs) is one kind of PTMs, which exerts comprehensive roles in cellular functions, including gene expression regulation, DNA repair, intracellular transport, stress responses, and tumorigenesis. With the development of the peptide enrichment approaches and MS technology, more than 6000 SUMOylated proteins and about 40 000 SUMO acceptor sites have been identified. In this review, we summarize several popular approaches that have been developed for the identification of SUMOylated proteins in human cells, and further compare their technical advantages and disadvantages. And we also introduce identification approaches of target proteins which are co‐modified by both SUMOylation and ubiquitylation. We highlight the emerging trends in the SUMOylation field as well. Especially, the advent of the clustered regularly interspaced short palindromic repeats/ Cas9 technique will facilitate the development of MS for SUMOylation identification. |
format | Online Article Text |
id | pubmed-6899701 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-68997012019-12-19 MS‐based strategies for identification of protein SUMOylation modification Sheng, Zenghua Wang, Xixi Ma, Yanni Zhang, Dan Yang, Yanfang Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang Electrophoresis Part V. Proteins, Proteomics and 2D Protein SUMOylation modification conjugated with small ubiquitin‐like modifiers (SUMOs) is one kind of PTMs, which exerts comprehensive roles in cellular functions, including gene expression regulation, DNA repair, intracellular transport, stress responses, and tumorigenesis. With the development of the peptide enrichment approaches and MS technology, more than 6000 SUMOylated proteins and about 40 000 SUMO acceptor sites have been identified. In this review, we summarize several popular approaches that have been developed for the identification of SUMOylated proteins in human cells, and further compare their technical advantages and disadvantages. And we also introduce identification approaches of target proteins which are co‐modified by both SUMOylation and ubiquitylation. We highlight the emerging trends in the SUMOylation field as well. Especially, the advent of the clustered regularly interspaced short palindromic repeats/ Cas9 technique will facilitate the development of MS for SUMOylation identification. John Wiley and Sons Inc. 2019-06-27 2019-11 /pmc/articles/PMC6899701/ /pubmed/31216068 http://dx.doi.org/10.1002/elps.201900100 Text en © 2019 The Authors. Electrophoresis published by WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Part V. Proteins, Proteomics and 2D Sheng, Zenghua Wang, Xixi Ma, Yanni Zhang, Dan Yang, Yanfang Zhang, Peng Zhu, Hongxia Xu, Ningzhi Liang, Shufang MS‐based strategies for identification of protein SUMOylation modification |
title | MS‐based strategies for identification of protein SUMOylation modification |
title_full | MS‐based strategies for identification of protein SUMOylation modification |
title_fullStr | MS‐based strategies for identification of protein SUMOylation modification |
title_full_unstemmed | MS‐based strategies for identification of protein SUMOylation modification |
title_short | MS‐based strategies for identification of protein SUMOylation modification |
title_sort | ms‐based strategies for identification of protein sumoylation modification |
topic | Part V. Proteins, Proteomics and 2D |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899701/ https://www.ncbi.nlm.nih.gov/pubmed/31216068 http://dx.doi.org/10.1002/elps.201900100 |
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