+ |
TOLLIP | down-regulates activity
binding
|
IRAK1 |
0.792 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251980 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10854325 |
Binding of IL-1 to its receptor results in rapid assembly of a membrane-proximal signalling complex that consists of two different receptor chains (IL-1Rs), IL-1RI and IL-1RAcP, the adaptor protein MyD88, the serine/threonine kinase IRAK and a new protein, which we have named Tollip. Here we show that, before IL-1β treatment, Tollip is present in a complex with IRAK, and that recruitment of Tollip–IRAK complexes to the activated receptor complex occurs through association of Tollip with IL-1RAcP. Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (and IL-1Rs) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IL1 Signaling |
+ |
IL1RAP | down-regulates activity
binding
|
TOLLIP |
0.622 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251979 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
10854325 |
Binding of IL-1 to its receptor results in rapid assembly of a membrane-proximal signalling complex that consists of two different receptor chains (IL-1Rs), IL-1RI and IL-1RAcP, the adaptor protein MyD88, the serine/threonine kinase IRAK and a new protein, which we have named Tollip. Here we show that, before IL-1β treatment, Tollip is present in a complex with IRAK, and that recruitment of Tollip–IRAK complexes to the activated receptor complex occurs through association of Tollip with IL-1RAcP. Co-recruited MyD88 then triggers IRAK autophosphorylation, which in turn leads to rapid dissociation of IRAK from Tollip (and IL-1Rs) |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | IL1 Signaling |