%0 Journal Article
%T Homodimerization of the c-Abl Protein Tyrosine Kinase<br>c-Abl蛋白酪氨酸激酶形成同源二聚体
%A WEI Ling
%A LIU Xuan
%A YI Yan-Ping
%A LI Chu-Fang
%A WANG Yun-Long
%A CAO Cheng
%A <br>魏玲
%A 刘萱
%A 易艳萍
%A 李楚芳
%A 王云龙
%A 曹诚
%J 生物工程学报
%D 2005
%I 
%X 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 prolinerich 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.
%K c-Abl
%K interaction
%K homodimers
%K SH3<br>c-Abl，相互作用，同源二聚体，SH3
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=BD1D4AFE87F7AA48&yid=2DD7160C83D0ACED&vid=659D3B06EBF534A7&iid=94C357A881DFC066&sid=6CDD207A90CE1EEC&eid=6C3EA4F7B6E5F836&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=20