PUBLICATION
Dynamic Phosphoproteome Profiling of Zebrafish Embryonic Fibroblasts During Cold Acclimation
- Authors
- Yan, J., Long, Y., Zhou, T., Ren, J., Li, Q., Song, G., Cui, Z.
- ID
- ZDB-PUB-191212-40
- Date
- 2019
- Source
- Proteomics 20(2): e1900257 (Journal)
- Registered Authors
- Cui, Zongbin, Li, Qing, Long, Yong, Song, Guili, Yan, Junjun
- Keywords
- cold acclimation, cold exposure, phosphoproteome profiling, signal transduction, zebrafish embryonic fibroblasts
- MeSH Terms
-
- Acclimatization/genetics
- Acclimatization/physiology
- Animals
- Cold Temperature
- Gene Expression Profiling
- Mitogen-Activated Protein Kinases/genetics
- Mitogen-Activated Protein Kinases/metabolism
- Phosphoproteins/genetics
- Phosphoproteins/metabolism*
- Phosphorylation/genetics
- Phosphorylation/physiology*
- Signal Transduction/genetics
- Signal Transduction/physiology
- Zebrafish
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- PubMed
- 31826332 Full text @ Proteomics
Citation
Yan, J., Long, Y., Zhou, T., Ren, J., Li, Q., Song, G., Cui, Z. (2019) Dynamic Phosphoproteome Profiling of Zebrafish Embryonic Fibroblasts During Cold Acclimation. Proteomics. 20(2):e1900257.
Abstract
Temperature affects almost all aspects of the fish life. To cope with low temperature within certain thermal windows, fish have evolved the ability of cold acclimation for survival. However, intracellular signaling events underlying cold acclimation in fish remain largely unknown. Here, we monitored the formation of cold acclimation in zebrafish embryonic fibroblasts (ZF4) and investigated the phosphorylation events during the process through a large-scale quantitative phosphoproteomic approach. In total, we identified 11,474 phosphorylation sites on 4,066 proteins and quantified 5,772 phosphosites on 2,519 proteins. Ser/Thr/Tyr phosphorylation in ZF4 cells accounted for 85.5%, 13.3% and 1.2% of total phosphosites, respectively. Among all phosphosites, 702 phosphosites on 510 proteins showed differential regulation during cold acclimation of ZF4 cells. These phosphosites were divided into six clusters according to their dynamic changes during cold exposure. Kinase-substrate prediction revealed that mitogen-activated protein kinase (MAPK) among the kinase groups is predominantly responsible for phosphorylation of these phosphosites. The differentially regulated phosphoproteins were functionally associated with various cellular processes such as regulation of actin cytoskeleton and MAPK signaling pathway. These data have enriched the database of protein phosphorylation sites in zebrafish and provided key clues for the elucidation of intracellular signaling networks during cold acclimation of fish. This article is protected by copyright. All rights reserved.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping