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Characterization of a cascade of protein interactions initiated at the IL-1 receptor.

Abstract：

:Prior studies have identified molecules involved in IL-1 signaling that transmit the extracellular stimulus to downstream kinase molecules causing altered transcriptional activity. Many of these investigations have relied heavily on ligand induced protein-protein interactions detected by immuno-coprecipitation to map the cascade of events from receptor binding to activation of downstream signaling intermediates. Direct protein interactions have not been commonly reported. An in vitro study was undertaken to better define the direct protein-protein interactions involved in IL-1 signaling. Results indicate that IRAK2 is capable of direct association with either IL-1R(I) or IL-1R(AcP). IRAK2 is also capable of associating directly with MyD88 by distinct regions. Finally, IRAK2 interactions with TRAF6 were mapped and demonstrate differences from more proximal signaling intermediates. A model is presented that reflects the specific molecular interactions responsible for recruiting signaling intermediates to the IL-1 receptor cytoplasmic domains.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Boch JA,Yoshida Y,Koyama Y,Wara-Aswapati N,Peng H,Unlu S,Auron PE

doi

10.1016/s0006-291x(03)00385-1

subject

Has Abstract

pub_date

2003-04-04 00:00:00

pages

525-31

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X03003851

journal_volume

303

pub_type

杂志文章

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