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