Dynamics of Dual Specificity Phosphatases and Their Interplay with Protein Kinases in Immune Signaling.
Animals
Biological Evolution
Blood Cells
/ metabolism
Dual-Specificity Phosphatases
/ metabolism
Humans
Immune System
/ cytology
Immunomodulation
Lymphoid Tissue
/ cytology
Mice
Protein Interaction Mapping
Protein Interaction Maps
Protein Kinases
/ metabolism
Proteome
Proteomics
/ methods
Signal Transduction
TLR signaling
hematopoietic cells
integrated omics analysis
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
27 Apr 2019
27 Apr 2019
Historique:
received:
05
03
2019
revised:
23
04
2019
accepted:
25
04
2019
entrez:
1
5
2019
pubmed:
1
5
2019
medline:
17
8
2019
Statut:
epublish
Résumé
Dual specificity phosphatases (DUSPs) have a well-known role as regulators of the immune response through the modulation of mitogen-activated protein kinases (MAPKs). Yet the precise interplay between the various members of the DUSP family with protein kinases is not well understood. Recent multi-omics studies characterizing the transcriptomes and proteomes of immune cells have provided snapshots of molecular mechanisms underlying innate immune response in unprecedented detail. In this study, we focus on deciphering the interplay between members of the DUSP family with protein kinases in immune cells using publicly available omics datasets. Our analysis resulted in the identification of potential DUSP-mediated hub proteins including MAPK7, MAPK8, AURKA, and IGF1R. Furthermore, we analyzed the association of DUSP expression with TLR4 signaling and identified VEGF, FGFR, and SCF-KIT pathway modules to be regulated by the activation of TLR4 signaling. Finally, we identified several important kinases including LRRK2, MAPK8, and cyclin-dependent kinases as potential DUSP-mediated hubs in TLR4 signaling. The findings from this study have the potential to aid in the understanding of DUSP signaling in the context of innate immunity. Further, this will promote the development of therapeutic modalities for disorders with aberrant DUSP signaling.
Identifiants
pubmed: 31035605
pii: ijms20092086
doi: 10.3390/ijms20092086
pmc: PMC6539644
pii:
doi:
Substances chimiques
Proteome
0
Protein Kinases
EC 2.7.-
Dual-Specificity Phosphatases
EC 3.1.3.48
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Research Council of Norway
ID : 263168
Organisme : Research Council of Norway
ID : 223255/F50
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