The I kappa B kinase complex (IKK) contains two kinase subunits, IKK alpha and IKK beta, necessary for I kappa B phosphorylation and NF-kappa B activation
The I kappa B kinase complex (IKK) contains two kinase subunits, IKK alpha and IKK beta, necessary for I kappa B phosphorylation and NF-kappa B activation
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DOI：
10.1016/s0092-8674(00)80406-7
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发表时间：
1997-10-17
期刊：
影响因子：
64.5
通讯作者：
Karin, M
中科院分区：
文献类型：
--
作者：
Zandi, E;Rothwarf, DM;Karin, M
最近，我们纯化了一个900 kDa的丝氨酸应答性I κ B激酶复合物（IKK），并对其亚基之一IKK α（丝氨酸激酶）进行了分子克隆。我们现在描述IKK复合物的第二个亚基IKK β的分子克隆和表征。IKK β与IKK α有50%的相同性，并且包含激酶结构域、亮氨酸拉链和螺旋-环-螺旋。虽然IKK α和IKK β可以进行同型相互作用，但它们也相互作用，并且功能性IKK复合物包含两种亚基。IKK α和IKK β的催化活性对I-κ B磷酸化和NF-κ B活化起重要作用。虽然IKK α和IKK β之间的相互作用可能是通过其亮氨酸拉链基序介导的，但其螺旋-环-螺旋基序可能涉及与必需的调节亚基的相互作用。
Recently we purified a 900 kDa cytokine-responsive I kappa B kinase complex (IKK) and molecularly cloned one of its subunits, IKK alpha, a serine kinase. We now describe the molecular cloning and characterization of IKK beta, a second subunit of the IKK complex. IKK beta is 50% identical to IKK alpha and like it contains a kinase domain, a leucine zipper, and a helix-loop-helix. Although IKK alpha and IKK beta can undergo homotypic interaction, they also interact with each other and the functional IKK complex contains both subunits. The catalytic activities of both IKK alpha and IKK beta make essential contributions to I kappa B phosphorylation and NF-kappa B activation. While the interactions between IKK alpha and IKK beta may be mediated through their leucine zipper motifs, their helix-loop-helix motifs may be involved in interactions with essential regulatory subunits.