Structure, function and regulation of the Toll/IL‐1 receptor adaptor proteins

Immunology and Cell Biology - Tập 85 Số 6 - Trang 411-419 - 2007
Tanya M Watters1, Elaine F. Kenny1, Luke O'neill1
1School of Biochemistry and Immunology, Trinity College Dublin, Ireland

Tóm tắt

The Toll/IL‐1 receptor (TIR) domain plays a central role in Toll‐like receptor (TLR) signalling. All TLRs contain a cytoplasmic TIR domain, which, upon activation, acts as a scaffold to recruit adaptor proteins. The adaptor proteins MyD88, Mal, TRIF, TRAM and SARM are also characterized by the presence of a TIR domain. MyD88, Mal, TRIF and TRAM associate with the TLRs via homophilic TIR domain interactions whereas SARM utilizes its TIR domain to negatively regulate TRIF. It is well established that the differential recruitment of adaptors to TLRs provides a significant amount of specificity to the TLR‐signalling pathways. Despite this, the TIR–TIR interface has not been well defined. However, structural studies have indicated the importance of TIR domain surfaces in mediating specific TIR–TIR interactions. Furthermore, recent findings regarding the regulation of adaptors provide further insight into the crucial role of the TIR domain in TLR signalling.

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Tài liệu tham khảo

10.1038/sj.cdd.4401850

10.1101/SQB.1989.054.01.003

10.1016/S0092-8674(00)80172-5

10.1038/41131

10.1126/science.282.5396.2085

10.1038/nature02761

10.1146/annurev.cellbio.21.122303.115827

10.1042/bst0280557

10.1016/j.cell.2006.02.015

10.1038/ni1112

10.1038/nri2079

10.1038/nri1630

10.1111/j.0105-2896.2005.00235.x

10.1073/pnas.0505077102

10.1126/science.1115253

10.1073/pnas.250476497

10.1074/jbc.M502074200

10.1073/pnas.0603245103

10.4049/jimmunol.169.1.10

10.1016/S0264-410X(03)00201-9

10.1016/j.it.2006.12.006

10.1016/S1471-4906(03)00242-4

10.1073/pnas.0306906101

10.1038/ni1207

10.1093/intimm/dxh097

10.1038/nature03253

10.1038/nri1916

10.1016/S0960-9822(02)00712-1

10.1074/jbc.273.20.12203

10.1016/S1074-7613(00)80402-1

10.1016/S1097-2765(00)80136-7

10.1016/S1074-7613(00)80086-2

10.4049/jimmunol.170.8.4237

10.1093/intimm/12.1.113

10.1074/jbc.M102262200

10.1084/jem.20021790

10.1146/annurev.biochem.76.060305.151318

10.1016/S0014-5793(03)00747-6

10.1073/pnas.082100399

10.1038/ncb0805-758

10.1016/S0092-8674(00)00126-4

10.1016/S1097-2765(00)80244-0

10.1101/gad.1228704

10.1038/35085597

10.1073/pnas.0403555101

10.1038/nature03547

10.1038/ni1118

10.1073/pnas.0406933101

10.1084/jem.20042372

10.1038/nature03308

10.1073/pnas.0607181103

10.1038/35092578

10.1038/ni0901-835

10.1038/nature01180

10.4049/jimmunol.169.12.6668

10.1038/ni886

10.1126/science.1087262

10.1073/pnas.2237236100

10.4049/jimmunol.171.8.4304

10.1038/nature04369

10.1038/nature04374

10.4049/jimmunol.174.1.27

10.1073/pnas.0308496101

10.4049/jimmunol.173.5.2913

10.1038/ni1061

10.1074/jbc.M506831200

10.1084/jem.20031023

10.1038/ni986

10.1038/ni1382

10.1016/0968-0004(94)90130-9

10.1073/pnas.95.2.588

10.1074/jbc.270.28.16514

Kuno K, 1993, Structure and function of the intracellular portion of the mouse interleukin 1 receptor (type I). Determining the essential region for transducing signals to activate the interleukin 8 gene, J Biol Chem, 268, 13510, 10.1016/S0021-9258(19)38679-X

10.1074/jbc.275.7.4670

10.1038/35040600

10.1074/jbc.M301742200

10.1038/337745a0

10.1074/jbc.M602057200

10.1073/pnas.0603804103

10.1016/S0006-291X(02)02581-0

10.4049/jimmunol.175.1.494

10.1073/pnas.0932746100

10.1002/eji.200535158

10.1074/jbc.C400289200

10.1016/j.cell.2006.05.014

10.1016/j.cell.2006.03.047

10.1074/jbc.M508892200

10.1038/ni1299

10.1073/pnas.0608100104

10.1016/j.molimm.2006.11.005

10.1038/ng1976

10.1073/pnas.0510041103

10.1073/pnas.0600462103

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Immunology and Cell Biology

Tập 85 Số 6

411-419

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