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 corr...

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Published inShengwu gongcheng xuebao Vol. 21; no. 5; p. 698
Main Authors Wei, Ling, Liu, Xuan, Yi, Yan-Ping, Li, Chu-Fang, Wang, Yun-Long, Cao, Cheng
Format Journal Article
LanguageEnglish
Published China 01.09.2005
Subjects
Humans
Protein Multimerization
Proto-Oncogene Proteins c-abl - genetics
Proto-Oncogene Proteins c-abl - metabolism
src Homology Domains
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Summary: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.
ISSN:1000-3061