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Cited by 1,290

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Signal-induced site-specific phosphorylation targets I kappa B alpha to the ubiquitin-proteasome pathway.

Open access
Chen, Z, Hagler, J, Palombella, V J, Melandri, F, Scherer, D, Ballard, D, Maniatis, T·1995·Genes & Development
DOI 10.1101/gad.9.13.1586
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Abstract

The transcription factor NF-kappa B is sequestered in the cytoplasm by the inhibitor protein I kappa B alpha. Extracellular inducers of NF-kappa B activate signal transduction pathways that result in the phosphorylation and subsequent degradation of I kappa B alpha. At present, the link between phosphorylation of I kappa B alpha and its degradation is not understood. In this report we provide evidence that phosphorylation of serine residues 32 and 36 of I kappa B alpha targets the protein to the ubiquitin-proteasome pathway. I kappa B alpha is ubiquitinated in vivo and in vitro following phosphorylation, and mutations that abolish phosphorylation and degradation of I kappa B alpha in vivo prevent ubiquitination in vitro. Ubiquitinated I kappa B alpha remains associated with NF-kappa B, and the bound I kappa B alpha is degraded by the 26S proteasome. Thus, ubiquitination provides a mechanistic link between phosphorylation and degradation of I kappa B alpha.

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Metadata

Authors
Chen, Z., Hagler, J., Palombella, V. J., Melandri, F., Scherer, D., Ballard, D., & Maniatis, T.
Venue
Genes & Development
Publisher
Cold Spring Harbor Laboratory
Published
1995-07-01
Volume
9
Issue
13
Pages
1586-1597
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
DOI
10.1101/gad.9.13.1586
OpenAlex
W2158708535
Cited by
1,290
References
2
Type
posted content
Language
en
Open access
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