Exip, a splicing variant of p38α, participates in interleukin‐1 receptor proximal complex and downregulates NF‐κB pathway
- 11 September 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 575 (1-3) , 136-140
- https://doi.org/10.1016/j.febslet.2004.08.050
Abstract
Here we report that Exip, but not p38α, binds to Toll interacting protein which is involved in interleukin‐1 (IL‐1) signaling pathway as a component of the receptor proximal complex and impaired NF‐κB activity. Moreover, Exip binds to another component of the complex, IL‐1 associating kinase. Exogenous‐expression of Exip resulted in downregulation of NF‐κB activities both in HeLa and HEK293T cells. Together, these results demonstrate that Exip can be a new component of NF‐κB pathway, and contribute to a comprehensive understanding of the signal transduction pathway in the inflammatory responses.Keywords
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