Structural aspects of protein kinase ASK1 regulation
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Review
PubMed
29066278
DOI
10.1016/j.jbior.2017.10.002
PII: S2212-4926(17)30163-X
Knihovny.cz E-resources
- MeSH
- Models, Biological MeSH
- Phosphorylation MeSH
- Humans MeSH
- MAP Kinase Kinase Kinase 5 genetics metabolism MeSH
- p38 Mitogen-Activated Protein Kinases genetics metabolism MeSH
- 14-3-3 Proteins genetics metabolism MeSH
- Thioredoxins genetics metabolism MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Review MeSH
- Names of Substances
- MAP Kinase Kinase Kinase 5 MeSH
- p38 Mitogen-Activated Protein Kinases MeSH
- 14-3-3 Proteins MeSH
- Thioredoxins MeSH
Apoptosis signal-regulating kinase 1 (ASK1, also known as MAP3K5), a member of the mitogen-activated protein kinase kinase kinase (MAP3K) family, activates the p38 mitogen-activated protein kinase and the c-Jun N-terminal kinase (JNK) signaling cascades in response to various stressors. ASK1 activity is tightly regulated through phosphorylation and interaction with various binding partners. However, the mechanistic details underlying the ASK1 regulation are still not fully understood. This review focuses on recent advances in structural studies of protein kinase ASK1 and on the insights they provide into its mechanism of regulation. In addition, we also discuss protein-protein interactions between ASK1 and its binding partners thioredoxin (TRX) and 14-3-3 protein.
References provided by Crossref.org
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
