Structural aspects of protein kinase ASK1 regulation
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu časopisecké články, přehledy
PubMed
29066278
DOI
10.1016/j.jbior.2017.10.002
PII: S2212-4926(17)30163-X
Knihovny.cz E-zdroje
- MeSH
- biologické modely MeSH
- fosforylace MeSH
- lidé MeSH
- MAP kinasa-kinasa-kinasa 5 genetika metabolismus MeSH
- mitogenem aktivované proteinkinasy p38 genetika metabolismus MeSH
- proteiny 14-3-3 genetika metabolismus MeSH
- thioredoxiny genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- MAP kinasa-kinasa-kinasa 5 MeSH
- mitogenem aktivované proteinkinasy p38 MeSH
- proteiny 14-3-3 MeSH
- thioredoxiny 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.
Citace poskytuje Crossref.org
The 14-3-3 Proteins as Important Allosteric Regulators of Protein Kinases
