Homodimerization of the c-Abl protein tyrosine kinase.
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.
Wei
Ling
L
Beijing Institute of Biotechnology, Academy of Military Medical Sciences, Beijing 100850, China.
Liu
Xuan
X
Yi
Yan-Ping
YP
Li
Chu-Fang
CF
Wang
Yun-Long
YL
Cao
Cheng
C
D006801:Humans; D055503:Protein Multimerization; D016315:Proto-Oncogene Proteins c-abl / Q000235:genetics / Q000378:metabolism*; D018909:src Homology Domains
D016315:Proto-Oncogene Proteins c-abl