PUBLICATION
Nuclear translocation of doublecortin-like protein kinase and phosphorylation of a transcription factor JDP2
- Authors
- Nagamine, T., Nomada, S., Onouchi, T., Kameshita, I., Sueyoshi, N.
- ID
- ZDB-PUB-140513-445
- Date
- 2014
- Source
- Biochemical and Biophysical Research Communications 446: 73-8 (Journal)
- Registered Authors
- Keywords
- Doublecortin, Doublecortin-like protein kinase, Hyperosmotic stress, Jun dimerization protein-2, Nuclear translocation
- MeSH Terms
-
- Active Transport, Cell Nucleus
- Animals
- Histones/metabolism
- Osmotic Pressure
- Phosphorylation
- Protein Interaction Domains and Motifs
- Protein Serine-Threonine Kinases/chemistry
- Protein Serine-Threonine Kinases/genetics
- Protein Serine-Threonine Kinases/metabolism*
- Recombinant Proteins/genetics
- Recombinant Proteins/metabolism
- Repressor Proteins/genetics
- Repressor Proteins/metabolism*
- Substrate Specificity
- Two-Hybrid System Techniques
- Zebrafish Proteins/chemistry
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism*
- PubMed
- 24582561 Full text @ Biochem. Biophys. Res. Commun.
Citation
Nagamine, T., Nomada, S., Onouchi, T., Kameshita, I., Sueyoshi, N. (2014) Nuclear translocation of doublecortin-like protein kinase and phosphorylation of a transcription factor JDP2. Biochemical and Biophysical Research Communications. 446:73-8.
Abstract
Doublecortin-like protein kinase (DCLK) is a microtubule-associated protein kinase predominantly expressed in brain. In a previous paper, we reported that zebrafish DCLK2 (zDCLK) was cleaved into two functional fragments; the N-terminal zDCLK(DC+SP) with microtubule-binding activity and the C-terminal zDCLK(kinase) with a Ser/Thr protein kinase activity. In this study, we demonstrated that zDCLK(kinase) was widely distributed in the cytoplasm and translocated into the nucleus when the cells were treated under hyperosmotic conditions with NaCl or mannitol. By two-hybrid screening using the C-terminal domain of DCLK, Jun dimerization protein 2 (JDP2), a nuclear transcription factor, was identified as zDCLK(kinase)-binding protein. Furthermore, JDP2 served as an efficient substrate for zDCLK(kinase) only when histone was present. These results suggest that the kinase fragment of DCLK is translocated into the nucleus upon hyperosmotic stresses and that the kinase efficiently phosphorylates JDP2, a possible target in the nucleus, with the aid of histones.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping