Strong anion exchange-mediated phosphoproteomics reveals extensive human non-canonical phosphorylation.
mass spectrometry
non-canonical phosphorylation
phosphohistidine
phosphoproteomics
strong anion exchange chromatography
Journal
The EMBO journal
ISSN: 1460-2075
Titre abrégé: EMBO J
Pays: England
ID NLM: 8208664
Informations de publication
Date de publication:
04 10 2019
04 10 2019
Historique:
received:
04
10
2018
revised:
24
07
2019
accepted:
01
08
2019
pubmed:
23
8
2019
medline:
7
1
2020
entrez:
22
8
2019
Statut:
ppublish
Résumé
Phosphorylation is a key regulator of protein function under (patho)physiological conditions, and defining site-specific phosphorylation is essential to understand basic and disease biology. In vertebrates, the investigative focus has primarily been on serine, threonine and tyrosine phosphorylation, but mounting evidence suggests that phosphorylation of other "non-canonical" amino acids also regulates critical aspects of cell biology. However, standard methods of phosphoprotein characterisation are largely unsuitable for the analysis of non-canonical phosphorylation due to their relative instability under acidic conditions and/or elevated temperature. Consequently, the complete landscape of phosphorylation remains unexplored. Here, we report an unbiased phosphopeptide enrichment strategy based on strong anion exchange (SAX) chromatography (UPAX), which permits identification of histidine (His), arginine (Arg), lysine (Lys), aspartate (Asp), glutamate (Glu) and cysteine (Cys) phosphorylation sites on human proteins by mass spectrometry-based phosphoproteomics. Remarkably, under basal conditions, and having accounted for false site localisation probabilities, the number of unique non-canonical phosphosites is approximately one-third of the number of observed canonical phosphosites. Our resource reveals the previously unappreciated diversity of protein phosphorylation in human cells, and opens up avenues for high-throughput exploration of non-canonical phosphorylation in all organisms.
Identifiants
pubmed: 31433507
doi: 10.15252/embj.2018100847
pmc: PMC6826212
doi:
Substances chimiques
Anions
0
Phosphopeptides
0
Phosphoproteins
0
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e100847Subventions
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/M023818/1
Pays : International
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/L005239/1
Pays : International
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/M012557/1
Pays : International
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/H007113/1
Pays : United Kingdom
Organisme : North West Cancer Research Fund (NWCR)
ID : CR1157
Pays : International
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/H007113/1
Pays : International
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/M025705/1
Pays : International
Organisme : UK Research and Innovation|Biotechnology and Biological Sciences Research Council (BBSRC)
ID : BB/R02216X/1
Pays : International
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/N021703/1
Pays : United Kingdom
Organisme : North West Cancer Research Fund (NWCR)
ID : CR1088
Pays : International
Organisme : North West Cancer Research Fund (NWCR)
ID : CR1037
Pays : International
Informations de copyright
© 2019 The Authors. Published under the terms of the CC BY 4.0 license.
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