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Updated: Feb 20, 2026

Assaying Protein Kinase Activity with Radiolabeled ATP
Published on: May 26, 2017
Structural aspects of protein kinase ASK1 regulation
Tomas Obsil1, Veronika Obsilova2
1Department of Physical and Macromolecular Chemistry, Faculty of Science, Charles University, 12843, Prague, Czech Republic; Department of Structural Biology of Signaling Proteins, Division BIOCEV, Institute of Physiology of the Czech Academy of Sciences, Prumyslova 595, 252 50, Vestec, Czech Republic.
Abstract:
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.
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