The STIR-domain superfamily in signal transduction, development and immunity

被引：225

作者：

Novatchkova, M ^{[1
]}

Leibbrandt, A ^{[1
]}

Werzowa, J ^{[1
]}

Neubüser, A ^{[1
]}

Eisenhaber, F ^{[1
]}

机构：

[1] Res Inst Mol Pathol, A-1030 Vienna, Austria

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2003年 / 28卷 / 05期

关键词：

D O I：

10.1016/S0968-0004(03)00067-7

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：

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.

引用

页码：226 / 229

页数：4

共 32 条

[11]

HEYUY A, 1992, J BIOL CHEM, V267, P2605

[12] Drosophila innate immunity: an evolutionary perspective [J].