Homodimerization of the c-Abl protein tyrosine kinase.
- Author:
Ling WEI
1
;
Xuan LIU
;
Yan-Ping YI
;
Chu-Fang LI
;
Yun-Long WANG
;
Cheng CAO
Author Information
1. Beijing Institute of Biotechnology, Academy of Military Medical Sciences, Beijing 100850, China.
- Publication Type:Journal Article
- MeSH:
Humans;
Protein Multimerization;
Proto-Oncogene Proteins c-abl;
genetics;
metabolism;
src Homology Domains
- From:
Chinese Journal of Biotechnology
2005;21(5):698-702
- CountryChina
- Language:English
-
Abstract:
The c-Abl nonreceptor tyrosine kinase is activated in the cellular responses to genotoxic, oxidative and other forms of stress. Using tagged forms of c-Abl, the present studies demonstrate that c-Abl forms homodimers in cells. The results show that the c-Abl N-terminal regions interact with the corresponding C-terminal regions of both partners in the dimmer. Specifically, the c-Abl SH3 domain binds to a proline-rich motif at amino acids 958-982 in the c-Abl C-terminal region. Deletion of the proline-rich motif disrupts dimmer formation. These findings provide the first evidence that c-Abl forms homodimers and indicate that homodimerization can contribute to the regulation of c-Abl activity.
