PUBLICATION
Influence of Ser/Pro-rich domain and kinase domain of doublecortin-like protein kinase on microtubule-binding activity
- Authors
- Nagamine, T., Shimomura, S., Sueyoshi, N., and Kameshita, I.
- ID
- ZDB-PUB-110207-8
- Date
- 2011
- Source
- Journal of biochemistry 149(5): 619-627 (Journal)
- Registered Authors
- Keywords
- doublecortin, doublecortin-like protein kinase, microtubule-binding activity, microtubule-associated protein, Ser/Pro-rich domain
- MeSH Terms
-
- Protein Structure, Tertiary
- Animals
- Proline/metabolism*
- Protein Binding
- COS Cells
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism*
- Zebrafish/anatomy & histology
- Zebrafish/metabolism
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Protein Serine-Threonine Kinases/chemistry*
- Protein Serine-Threonine Kinases/genetics
- Protein Serine-Threonine Kinases/metabolism*
- Chlorocebus aethiops
- Microtubule-Associated Proteins/genetics
- Microtubule-Associated Proteins/metabolism
- Microtubules/metabolism*
- Neuropeptides/genetics
- Neuropeptides/metabolism
- Serine/metabolism*
- PubMed
- 21278387 Full text @ J. Biochem.
Citation
Nagamine, T., Shimomura, S., Sueyoshi, N., and Kameshita, I. (2011) Influence of Ser/Pro-rich domain and kinase domain of doublecortin-like protein kinase on microtubule-binding activity. Journal of biochemistry. 149(5):619-627.
Abstract
Doublecortin-like protein kinase (DCLK) is a Ser/Thr protein kinase predominantly expressed in brain. DCLK is composed of three functional domains; the N-terminal doublecortin-like (DC) domain, the C-terminal kinase domain, and Ser/Pro-rich (SP) domain in between DC and kinase domains. Although the DC domain is known to mediate microtubule association, functional roles of the SP domain and the kinase domain on microtubule association is not known. In this study, we investigated the microtubule-binding activity of zebrafish DCLK (zDCLK) using various deletion mutants and chimeric proteins. The microtubule-binding activity of various mutants of zDCLK was assessed both by immunocytochemical analysis and by biochemical analysis using detergent extraction method. When the kinase domain was removed from zDCLK, the microtubule-binding activity was significantly enhanced. Although the zDCLK(DC+SP) mutant showed a strong microtubule-binding activity, the DC domain alone showed much lower microtubule-binding activity, indicating that the SP domain of zDCLK plays a role in enhancing microtubule-binding activity of the DC domain. These results suggest that both the kinase domain and the SP domain are involved in regulating the microtubule-binding activity of DCLK.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping