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Exip, a splicing variant of p38α, participates in interleukin‐1 receptor proximal complex and downregulates NF‐κB pathway
Author(s) -
Yagasaki Yuki,
Sudo Tatsuhiko,
Osada Hiroyuki
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.050
Subject(s) - signal transduction , microbiology and biotechnology , downregulation and upregulation , p38 mitogen activated protein kinases , nf κb , interleukin 1 receptor , receptor , chemistry , hek 293 cells , toll like receptor , biology , interleukin , cytokine , mapk/erk pathway , gene , immunology , innate immune system , biochemistry
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.