Self-association of LIM-kinase 1 mediated by the interaction between an N-terminal LIM domain and a C-terminal kinase domain

被引:31
作者
Hiraoka, J
Okano, I
Higuchi, O
Yang, N
Mizuno, K
机构
[1] KYUSHU UNIV,FAC SCI,DEPT BIOL,FUKUOKA 81281,JAPAN
[2] JAPAN SCI & TECHNOL CORP,PRESTO,KYOTO 61902,JAPAN
关键词
protein kinase; LIM motif; LIMK; dimerization;
D O I
10.1016/S0014-5793(96)01303-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
LIM-kinase 1 (LIMK1) and 2 (LIMK2) are members of a novel class of protein kinases containing two LIM motifs at the N-terminus. The LIM motif is thought to be involved in protein-protein interactions. We report here evidence that LIMK1 self-associates and also associates with LIMK2. In vivo and in vitro binding analyses using variously deleted mutants of LIMK1 revealed that the self-association of LIMK1 was caused by interaction between the N-terminal LIM domain and the C-terminal kinase domain. The association of LIMK1 with itself and with LIMK2 is important for understanding how activities and functions of LIMK family kinases are regulated.
引用
收藏
页码:117 / 121
页数:5
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