Phosphorylation of human IκB-α on serines 32 and 36 controls IκB-α proteolysis and NF-κB activation in response to diverse stimuli

EMBO Journal

Volumn 14, Issue 12, 1995, Pages 2876-2883

  Traenckner, E Britta Mareen ^a   Pahl, Heike L ^a   Henkel, Thomas ^b   Schmidt, Kerstin N ^a   Wilk, Sherwin ^c   A baeuerle, Patrick ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

^b MOUNT SINAI MEDICAL CENTER   (United States)

^c MediGene AG   (Germany)

Author keywords

I B ; NF B; Phosphorylation; Proteolysis

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MUTANT PROTEIN; OKADAIC ACID; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN SUBUNIT; SERINE; TRANSCRIPTION FACTOR; TUMOR NECROSIS FACTOR ALPHA;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; HELA CELL; HUMAN; HUMAN CELL; POINT MUTATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; STRUCTURE ACTIVITY RELATION; TRANSACTIVATION;

EUKARYOTA;

EID: 0028978032     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1002/j.1460-2075.1995.tb07287.x     Document Type: Article

References (12)

1. Alkalay,I., Yaron.A., Hatzubsai,A., Jung.S., Avraham,A., Gerlitz,O., Pashut-Lavon.I. and Ben-Neriah,Y. (1995) In vivo stimulation of 1κB phosphorylation is not sufficient to activate NF-κB. Mol. Cell. Dial., in press.
2. Baeuerle,P.A. and Baltimore,D. (1988) 1κB: a specific inhibitor of the NF-κB transcription factor. Science. 242, 540-546.
3. Baeuerle,P.A. and Henkel, T. (1994) Function and activation of NF-B κ in the immune system. Anna. Rev. Immunol., 12, 141-179.
4. Beg,A.A. and Baldwin,A.S. (1993) The IκB proteins: multifunctional regulators of Rel/NF-κB transcription factors. Genes Dev., 7, 1564-1570.
5. Beg,A.A., Finco.T.S., Nantermet,P.V. and Baldwin,A.S.Jr (1993) Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκB-α: a mechanism for NF-κB activation. Mol. Cell. Biol., 13. 3301-3310.
6. Blank,V., Kourilsky,P. and Israël,A. (1992) NF-κB and related proteins: Rel/dorsal homologies meet ankyrin-like repeats. Trench Biochem. Sci., 17, 135-140.
7. Sun.S.-C, Elwood, Béraud,C. and Greene,W.C. (1994b) Human Tcell leukemia virus type I tax activation of NF-κB/Rel involves phosphorylation and degradation of IκBα and RelA(p65)-mediated induction of the c-rel gene. Mol. Cell. Biol., 14. 7377-7384.
8. Tewari,M., Dobrzanski,P., Mohn,K.L., Cressman,D.F., Hsu.J.C., Bravo,R. and Taub.R. (1992) Rapid induction in regenerating liver of RI./IF-1 (an 1κB that inhibits NF-κB, RelB-p50, and c-Rel-p50) and PHF, a novel κB site binding complex. Mol. Cell. Biol., 12. 2898-2908
9. Traenckner,E.B.-M., Wilk,S. and Baeuerle,P.A. (1994) A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB. EMBO J., 13, 5433-5441.
10. Traenckner,E.B.-M. and Baeuerle,P.A. (1995) Appearance of ubiquitinconjugated IκB-α during its phosphorylation-induced degradation. J. Cell. Sci., in press.
11. Whalen,A.M. and Steward,R. (1993) Dissociation of the dorsal-cactus complex and phosphorylation of the dorsal protein correlate with the nuclear localization of dorsal. J. Cell. Biol., 123, 523-534.
12. Wigler,M., Pellicer,A., Silverstein,A. and Axel,R. (1978) Biochemical transfer of single-copy eukaryotic genes using total cellular DNA as donor. Cell, 14, 725-731.