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Cutting Edge |
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine and Walther Cancer Institute, Indianapolis, IN 46202
Pellino is a Drosophila protein originally
isolated in a two-hybrid screen for proteins interacting with the
serine/threonine kinase, pelle. Although mammalian homologs have been
identified in mouse and man, the function of pellino is as yet unknown.
In this study, the cloning, expression pattern, and a preliminary
characterization of mouse pellino-2 is described. These studies reveal
that mouse pellino-2 is expressed during embryogenesis and in a
tissue-restricted manner in the adult. IL-1 induces the association of
mouse pellino-2 with the mouse pelle-like kinase/IL-1R-associated
kinase protein, a mammalian homolog of pelle. Ectopic pellino-2
expression did not result in NF-
B activation. However, ectopic
expression of a mouse pellino-2 antisense construct inhibited IL-1 or
LPS-induced activation of NF-
B-dependent IL-8 promoter activity. Our
data reveal that mouse pellino-2 is a tissue-restricted component of a
signaling pathway that couples the mouse pelle-like
kinase/IL-1R-associated kinase protein to IL-1- or LPS-dependent
signaling.
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