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© Research
Publication : Bioscience, biotechnology, and biochemistry

The kinase domain of CK1δ can be phosphorylated by Chk1.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Bioscience, biotechnology, and biochemistry - 01 Sep 2019

Böhm T, Meng Z, Haas P, Henne-Bruns D, Rachidi N, Knippschild U, Bischof J,

Link to Pubmed [PMID] – 31094292

Link to DOI – 10.1080/09168451.2019.1617105

Biosci Biotechnol Biochem 2019 Sep; 83(9): 1663-1675

Members of the casein kinase 1 (CK1) family are key regulators in numerous cellular signal transduction pathways and in order to prevent the development of certain diseases, CK1 kinase activity needs to be tightly regulated. Modulation of kinase activity by site-specific phosphorylation within the C-terminal regulatory domain of CK1δ has already been shown for several cellular kinases. By using biochemical methods, we now identified residues T161, T174, T176, and S181 within the kinase domain of CK1δ as target sites for checkpoint kinase 1 (Chk1). At least residues T176 and S181 show full conservation among CK1δ orthologues from different eukaryotic species. Enzyme kinetic analysis furthermore led to the hypothesis that site-specific phosphorylation within the kinase domain finally contributes to fine-tuning of CK1δ kinase activity. These data provide a basis for the extension of our knowledge about the role of site-specific phosphorylation for regulation of CK1δ and associated signal transduction pathways.