Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition
Arginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus i...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-05-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/ncomms15571 |
| _version_ | 1818341991548715008 |
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| author | Evgenia Shishkova Hao Zeng Fabao Liu Nicholas W. Kwiecien Alexander S. Hebert Joshua J. Coon Wei Xu |
| author_facet | Evgenia Shishkova Hao Zeng Fabao Liu Nicholas W. Kwiecien Alexander S. Hebert Joshua J. Coon Wei Xu |
| author_sort | Evgenia Shishkova |
| collection | DOAJ |
| description | Arginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus in substrate recognition. |
| first_indexed | 2024-12-13T16:07:35Z |
| format | Article |
| id | doaj.art-222565a41f79486c861ca88378e98eac |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-13T16:07:35Z |
| publishDate | 2017-05-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-222565a41f79486c861ca88378e98eac2022-12-21T23:39:00ZengNature PortfolioNature Communications2041-17232017-05-018111310.1038/ncomms15571Global mapping of CARM1 substrates defines enzyme specificity and substrate recognitionEvgenia Shishkova0Hao Zeng1Fabao Liu2Nicholas W. Kwiecien3Alexander S. Hebert4Joshua J. Coon5Wei Xu6The Department of Biomolecular Chemistry, University of Wisconsin – MadisonMcArdle Laboratory for Cancer Research, University of Wisconsin – MadisonMcArdle Laboratory for Cancer Research, University of Wisconsin – MadisonThe Genome Center of Wisconsin, University of Wisconsin – MadisonThe Genome Center of Wisconsin, University of Wisconsin – MadisonThe Department of Biomolecular Chemistry, University of Wisconsin – MadisonMcArdle Laboratory for Cancer Research, University of Wisconsin – MadisonArginine methylation is an abundant post-translational modification catalysed by protein arginine methyltransferases (PRMTs). Here the authors use quantitative mass spectrometry to globally profile the substrates of the PRMT CARM1 in breast cancer cells, and establish a role for CARM1’s N-terminus in substrate recognition.https://doi.org/10.1038/ncomms15571 |
| spellingShingle | Evgenia Shishkova Hao Zeng Fabao Liu Nicholas W. Kwiecien Alexander S. Hebert Joshua J. Coon Wei Xu Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition Nature Communications |
| title | Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition |
| title_full | Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition |
| title_fullStr | Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition |
| title_full_unstemmed | Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition |
| title_short | Global mapping of CARM1 substrates defines enzyme specificity and substrate recognition |
| title_sort | global mapping of carm1 substrates defines enzyme specificity and substrate recognition |
| url | https://doi.org/10.1038/ncomms15571 |
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