A human kinase yeast array for the identification of kinases modulating phosphorylation-dependent protein-protein interactions.
U5 spliceosome
estrogen receptor
kinase signaling
protein networks
yeast two-hybrid
Journal
Molecular systems biology
ISSN: 1744-4292
Titre abrégé: Mol Syst Biol
Pays: England
ID NLM: 101235389
Informations de publication
Date de publication:
03 2022
03 2022
Historique:
revised:
28
01
2022
received:
19
11
2021
accepted:
31
01
2022
entrez:
28
2
2022
pubmed:
1
3
2022
medline:
3
5
2022
Statut:
ppublish
Résumé
Protein kinases play an important role in cellular signaling pathways and their dysregulation leads to multiple diseases, making kinases prime drug targets. While more than 500 human protein kinases are known to collectively mediate phosphorylation of over 290,000 S/T/Y sites, the activities have been characterized only for a minor, intensively studied subset. To systematically address this discrepancy, we developed a human kinase array in Saccharomyces cerevisiae as a simple readout tool to systematically assess kinase activities. For this array, we expressed 266 human kinases in four different S. cerevisiae strains and profiled ectopic growth as a proxy for kinase activity across 33 conditions. More than half of the kinases showed an activity-dependent phenotype across many conditions and in more than one strain. We then employed the kinase array to identify the kinase(s) that can modulate protein-protein interactions (PPIs). Two characterized, phosphorylation-dependent PPIs with unknown kinase-substrate relationships were analyzed in a phospho-yeast two-hybrid assay. CK2α1 and SGK2 kinases can abrogate the interaction between the spliceosomal proteins AAR2 and PRPF8, and NEK6 kinase was found to mediate the estrogen receptor (ERα) interaction with 14-3-3 proteins. The human kinase yeast array can thus be used for a variety of kinase activity-dependent readouts.
Identifiants
pubmed: 35225431
doi: 10.15252/msb.202110820
pmc: PMC8883442
doi:
Substances chimiques
Proteins
0
Saccharomyces cerevisiae Proteins
0
Protein Kinases
EC 2.7.-
NEK6 protein, human
EC 2.7.11.1
NIMA-Related Kinases
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e10820Subventions
Organisme : Austrian Science Fund FWF
ID : P 34316
Pays : Austria
Informations de copyright
©2022 The Authors. Published under the terms of the CC BY 4.0 license.
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