Tyrosine phosphorylation of I kappa B-alpha activates NF-kappa B without proteolytic degradation of I kappa B-alpha

被引：620

作者：

Imbert, V ^{[1
]}

Rupec, RA ^{[1
]}

Livolsi, A ^{[1
]}

Pahl, HL ^{[1
]}

Traenckner, EBM ^{[1
]}

MuellerDieckmann, C ^{[1
]}

Farahifar, D ^{[1
]}

Rossi, B ^{[1
]}

Auberger, P ^{[1
]}

Baeuerle, PA ^{[1
]}

Peyron, JF ^{[1
]}

机构：

[1] UNIV FREIBURG, INST BIOCHEM, D-79104 FREIBURG, GERMANY

来源：

CELL | 1996年 / 86卷 / 05期

关键词：

D O I：

10.1016/S0092-8674(00)80153-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The transcription factor NF-kappa B regulates genes participating in immune and inflammatory responses. In T lymphocytes, NF-kappa B is sequestered in the cytosol by the inhibitor I kappa B-alpha and released after serine phosphorylation of I kappa B-alpha that regulates its ubiquitin-dependent degradation. We report an alternative mechanism of NF-kappa B activation. Stimulation of Jurkat T cells with the protein tyrosine phosphatase inhibitor and T cell activator pervanadate led to NF-kappa B activation through tyrosine phosphorylation but not degradation of I kappa B-alpha. Pervanadate-induced I kappa B-alpha phosphorylation and NF-kappa B activation required expression of the T cell tyrosine kinase p56(lck). Reoxygenation of hypoxic cells appeared as a physiological effector of I kappa B-alpha tyrosine phosphorylation. Tyrosine phosphorylation of I kappa B-alpha represents a proteolysis-independent mechanism of NF-kappa B activation that directly couples NF-kappa B to cellular tyrosine kinase.

引用

页码：787 / 798

页数：12

共 47 条

[1]

ALKALAY I, 1995, MOL CELL BIOL, V15, P1294

[2]

BAEUERLE PA, 1994, ANNU REV IMMUNOL, V12, P141, DOI 10.1146/annurev.immunol.12.1.141

[3] I-KAPPA-B - A SPECIFIC INHIBITOR OF THE NF-KAPPA-B TRANSCRIPTION FACTOR [J].