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Sites on FIP-3 (NEMO/IKKgamma) essential for its phosphorylation and NF-kappaB modulating activity.

Abstract：

:FIP-3 (NEMO/IKKgamma) is an essential modulator of the activity of NF-kappaB by mechanisms that include alterations in the phosphorylation, ubiquination, and degradation of IkappaBalpha. The multiple protein-protein interactions of FIP-3 (NEMO/IKKgamma) in a high molecular weight IKK complex indicated that this protein may be a link between some of the receptor-proximal upstream signal transduction molecules such as RIP and the downstream effects on IkappaBalpha. Although FIP-3 (NEMO/IKKgamma) has no intrinsic kinase activity, it has been shown to increase the kinase activity of IKKbeta. In this manuscript, the results of serine to alanine mutations at five sites on FIP-3 (NEMO/IKKgamma) are described, and functional assays demonstrated that two of these mutants affect both the phosphorylation and kinase activity of IKKbeta. Protein kinase Calpha appeared to be the kinase that was required for the posttranslational modification of FIP-3 (NEMO/IKKgamma). One of the serine targets of the protein kinase Calpha enzyme at amino acid 141 was within a leucine zipper-like sequence of FIP-3 (NEMO/IKKgamma), which might affect its interactions with other proteins on the signal transduction pathway. The second serine, which augmented the inhibition, was at amino acid 85 within the FIP-3 (NEMO/IKKgamma) interaction site with IKKbeta. When both serines were mutated simultaneously, the effect on IKKbeta and IkappaBalpha phosphorylation was more profoundly affected.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Tarassishin L,Horwitz MS

doi

10.1006/bbrc.2001.5197

subject

Has Abstract

pub_date

2001-07-13 00:00:00

pages

555-60

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95197-6

journal_volume

285

pub_type

杂志文章

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