Related Experiment Video
Updated: Jun 25, 2026

11:13
Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
Exploring the multifaceted Dbf4-dependent kinase from temporal, spatial, and substrate repertoire perspectives.
Lorenzo Galanti1,2, Boris Pfander3
1Cell Biology, TU Dortmund Life Science Center (DOLCE), Department of Chemistry and Chemical Biology, TU Dortmund University, Dortmund, Germany.
Communications Biology
|June 23, 2026
Summary
The Dbf4-dependent kinase (DDK) is a crucial enzyme for DNA replication and genome stability. This review redefines DDK as a multifunctional kinase with roles beyond replication, highlighting its therapeutic potential in cancer therapy.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The Dbf4-dependent kinase (DDK), comprising Cdc7 and Dbf4 subunits, is recognized as a key regulator of DNA replication initiation.
- Its precise roles in cell cycle progression and genome maintenance are under ongoing investigation.
Purpose of the Study:
- To review the multifaceted functions of DDK by examining its temporal regulation, spatial organization, and substrate interactions.
- To re-evaluate DDK's role in cellular processes beyond DNA replication.
Main Methods:
- Literature review integrating cell cycle studies, chromosome organization research, and substrate analysis.
- Analysis of DDK's targeting of proteins involved in DNA replication, chromosome segregation, DNA damage response, and homologous recombination.
Main Results:
- DDK exhibits complex temporal regulation throughout the cell cycle.
- DDK is spatially organized on chromosomes, indicating precise localization for its functions.
- DDK targets a diverse set of proteins, extending its known functions beyond DNA replication initiation.
Conclusions:
- DDK is a multifunctional genome integrity kinase coordinating cell cycle progression and genome stability.
- DDK's expanded substrate repertoire and regulatory mechanisms offer significant therapeutic potential for cancer treatment.
Related Concept Videos
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

