The STIR-domain superfamily in signal transduction, development and immunity
The STIR-domain superfamily in signal transduction, development and immunity
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DOI：
10.1016/s0968-0004(03)00067-7
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发表时间：
2003-05-01
影响因子：
13.8
通讯作者：
Eisenhaber, F
中科院分区：
文献类型：
--
作者：
Novatchkova, M;Leibbrandt, A;Eisenhaber, F
我们在真核生物和细菌的跨膜受体（包括SEFs、IL 17 Rs）和可溶性因子（包括CIKS/ACT 1）中鉴定了一个保守的序列片段--SEFIR结构域。该序列结构域是新的STIR结构域超家族的一部分，其还包含已知介导TIR-TIR同型相互作用的TIR结构域。在TOLL/IL 1 R样途径中，受体的胞质定位TIR结构域和可溶性衔接子的TIR结构域物理相互作用并激活信号传导。SEFIR和TIR结构域之间的相似性涉及TIR结构域的保守框1和2，其涉及同型二聚化，但SEFIR结构域和TIR序列框3之间没有序列相似性。通过类比，我们认为SEFIR结构域蛋白作为Toll/IL-1 R类似通路的信号传导组分起作用，并且它们的SEFIR结构域介导通路组分之间的物理蛋白质-蛋白质相互作用。
We have identified a conserved sequence segment in transmembrane receptors (including SEFs, IL17Rs) and soluble factors (including CIKS/ACT1) in eukaryotes and bacteria - the SEFIR domain. This sequence domain is part of the new STIR domain superfamily comprising also the TIR domain known to mediate TIR-TIR homotypic interactions. In TOLL/IL1R-like pathways, the cytoplasmically localized TIR domain of a receptor and the TIR domain of a soluble adaptor interact physically and activate signalling. The similarity between the SEFIR and TIR domains involves the conserved boxes 1 and 2 of the TIR domain that are implicated in homotypic dimerization, but there is no sequence similarity between SEFIR domains and the TIR sequence box 3. By analogy, we suggest that SEFIR-domain proteins function as signalling components of Toll/IL-1R-similar pathways and that their SEFIR domain mediates physical protein-protein interactions between pathway components.