Abstract
Death-associated protein kinase (DAPK) is a calmodulin-regulated serine/threonine protein kinase associated with neuronal cell death in animal models of disease. The recent determination of the 1.5Å crystal structure of the catalytic kinase domain of DAPK, the discovery of amino acid sequence motifs with sites that are preferentially phosphorylated by this kinase, and the development of a quantitative enzyme activity assay provide a firm foundation for future studies into its regulation, the identification of its physiological substrates, and discovery of inhibitors. We summarize the relevant background and ongoing investigations that will increase our understanding of the role and regulation of this prototype death-associated kinase.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 217-224 |
| Number of pages | 8 |
| Journal | Pharmacology and Therapeutics |
| Volume | 93 |
| Issue number | 2-3 |
| DOIs | |
| State | Published - 2002 |
Funding
This work has been supported in part by grants from the Alzheimer's Association and the Institute for the Study of Aging. A.V.V. and A.M.S. are postdoctoral and predoctoral scholars, respectively, in drug discovery research supported by a training grant from the National Institutes of Health (T32 AG00260).
Keywords
- Apoptosis
- Calmodulin
- Chemical genomics
- Drug discovery
- Kinase inhibitors
- Protein kinase
ASJC Scopus subject areas
- Pharmacology (medical)
- Pharmacology
