Hiraoka J, Okano I, Higuchi O, Yang N, Mizuno K
Department of Biology, Faculty of Science, Kyushu University, Fukuoka, Japan.
FEBS Lett. 1996 Dec 9;399(1-2):117-21. doi: 10.1016/s0014-5793(96)01303-8.
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 LIMKI 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.
LIM激酶1（LIMK1）和2（LIMK2）是一类新型蛋白激酶的成员，在其N端含有两个LIM基序。LIM基序被认为参与蛋白质-蛋白质相互作用。我们在此报告LIMK1能自我结合且也能与LIMK2结合的证据。使用LIMK1各种缺失突变体进行的体内和体外结合分析表明，LIMK1的自我结合是由N端LIM结构域与C端激酶结构域之间的相互作用引起的。LIMK1与其自身以及与LIMK2的结合对于理解LIMK家族激酶的活性和功能如何被调节很重要。
