FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation.
FIST/HIPK3: a Fas/FADD-interacting serine/threonine kinase that induces FADD phosphorylation and inhibits fas-mediated Jun NH(2)-terminal kinase activation.
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DOI：
10.1084/jem.192.8.1165
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发表时间：
2000-10-16
期刊：
影响因子：
--
通讯作者：
Tschopp J
中科院分区：
文献类型：
--
作者：
Rochat-Steiner V;Becker K;Micheau O;Schneider P;Burns K;Tschopp J
Fas是一种细胞表面死亡受体，可发出凋亡信号。已经鉴定了几种与Fas的胞质死亡结构域结合的蛋白质。Fas相关死亡结构域（FADD），其将Fas偶联至半胱天冬酶原-8，和Daxx，其将Fas偶联至Jun NH 2-末端激酶途径，独立地结合至Fas死亡结构域。我们已经确定了一个130 kD的激酶命名为Fas相互作用丝氨酸/苏氨酸激酶/同源域相互作用蛋白激酶（FIST/HIPK 3）作为一种新的Fas相互作用蛋白。与Fas的结合由蛋白质COOH末端的保守序列介导。FIST/HIPK 3在哺乳动物组织中广泛表达，并定位于细胞核和细胞质中。在转染的细胞系中，FIST/HIPK 3引起FADD磷酸化，从而促进FIST/HIPK 3-FADD-Fas相互作用。尽管Fas配体诱导的Jun NH 2-末端激酶的活化受到过表达的活性FIST/HIPK 3的损害，但细胞死亡不受影响。这些结果表明，Fas相关的FIST/HIPK 3调节Fas的两个主要信号通路之一。
Fas is a cell surface death receptor that signals apoptosis. Several proteins have been identified that bind to the cytoplasmic death domain of Fas. Fas-associated death domain (FADD), which couples Fas to procaspase-8, and Daxx, which couples Fas to the Jun NH2-terminal kinase pathway, bind independently to the Fas death domain. We have identified a 130-kD kinase designated Fas-interacting serine/threonine kinase/homeodomain-interacting protein kinase (FIST/HIPK3) as a novel Fas-interacting protein. Binding to Fas is mediated by a conserved sequence in the COOH terminus of the protein. FIST/HIPK3 is widely expressed in mammalian tissues and is localized both in the nucleus and in the cytoplasm. In transfected cell lines, FIST/HIPK3 causes FADD phosphorylation, thereby promoting FIST/HIPK3–FADD–Fas interaction. Although Fas ligand–induced activation of Jun NH2-terminal kinase is impaired by overexpressed active FIST/HIPK3, cell death is not affected. These results suggest that Fas-associated FIST/HIPK3 modulates one of the two major signaling pathways of Fas.
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