Influence of Ser/Pro-rich domain and kinase domain of double cortin-like protein kinase on microtubule-binding activity

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 D...

Full description

Saved in:
Bibliographic Details
Published in:Journal of biochemistry (Tokyo) 2011-05, Vol.149 (5), p.619-627
Main Authors: Nagamine, Tadashi, Shimomura, Sachiko, Sueyoshi, Noriyuki, Kameshita, Isamu
Format: Article
Language:English
Subjects:
Animals
Cercopithecus aethiops
COS Cells
Danio rerio
Freshwater
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Microtubules - metabolism
Neuropeptides - genetics
Neuropeptides - metabolism
Proline - metabolism
Protein Binding
Protein Structure, Tertiary
Protein-Serine-Threonine Kinases - chemistry
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Serine - metabolism
Zebrafish - anatomy & histology
Zebrafish - metabolism
Zebrafish Proteins - chemistry
Zebrafish Proteins - genetics
Zebrafish Proteins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0021-924X
1756-2651
DOI:10.1093/jb/mvr013