Site-Specific Phosphorylation of IκBα by a Novel Ubiquitination-Dependent Protein Kinase Activity
@article{Chen1996SiteSpecificPO, title={Site-Specific Phosphorylation of I$\kappa$B$\alpha$ by a Novel Ubiquitination-Dependent Protein Kinase Activity}, author={Zhijian J. Chen and Lana A. Parent and Tom Maniatis}, journal={Cell}, year={1996}, volume={84}, pages={853-862} }
959 Citations
cRel-TD kinase: a serine/threonine kinase binding in vivo and in vitro c-Rel and phosphorylating its transactivation domain
- Biology, Computer ScienceOncogene
- 2000
Pull-down and immunoprecipitation experiments showing that a mammalian 66 kDa protein kinase binds murine c-Rel, both in vitro and in vivo, suggests a proline-directed serine/threonine substrate specificity similar to MAP kinases.
Site-specific Tyrosine Phosphorylation of IκBα Negatively Regulates Its Inducible Phosphorylation and Degradation*
- BiologyThe Journal of Biological Chemistry
- 1996
The results demonstrate that inducible phosphorylation and degradation of IκBα are negatively regulated by phosphorylated at Tyr-42, thus preventing NF-κB activation.
Inducible Degradation of IκBα by the Proteasome Requires Interaction with the F-box Protein h-βTrCP*
- BiologyThe Journal of Biological Chemistry
- 1999
It is indicated that βTrCP is the adaptor protein required for IκBα recognition by the SCFβTrCP E3 complex that ubiquitinates Iκbα and makes it a substrate for the proteasome.
Signal-induced Ubiquitination of IκB Kinase-β*
- Biology, ChemistryJournal of Biological Chemistry
- 2003
Evidence is reported that pathologic and physiologic inducers of NF-κB target IKKβ for conjugation to ubiquitin (Ub) in mammalian cells, indicating an important mechanistic link between phosphorylation, ubiquitination, and the biologic action of IKK β.
Activation of the IκB Kinase Complex by TRAF6 Requires a Dimeric Ubiquitin-Conjugating Enzyme Complex and a Unique Polyubiquitin Chain
- Biology, ChemistryCell
- 2000
SCFβ-TRCP and phosphorylation dependent ubiquitination of IκBα catalyzed by Ubc3 and Ubc4
- Biology, ChemistryOncogene
- 2000
The results suggest that the cullin specificity of the SCF complex may reflect its ability to associate with Rbx1, and suggest that ubiquitin is transferred directly from the Ubc to phospho-IκBα in a SCFβ-TRCP dependent reaction.
Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IκBα
- Biology, Chemistry
- 1997
It is proposed that mE2 is directly involved in the ubiquitin conjugation of IκBα, a pivotal step in its degradation pathway, and tumor necrosis factor-α-inducible NF-κB activity was diminished.
The 90-kDa Ribosomal S6 Kinase (pp90rsk) Phosphorylates the N-terminal Regulatory Domain of IκBα and Stimulates Its Degradation in Vitro *
- BiologyThe Journal of Biological Chemistry
- 1997
It is shown that pp90rsk, but not pp70S6K or MAP kinase, phosphorylates the regulatory N terminus of IκBα principally on serine 32 and triggers effective Iκ bα degradation in vitro, suggesting that more than a single Iκbα kinase exists within the cell and that these Iκ Bα kinases are differentially activated by different NF-κB inducers.
Enzymes Catalyzing Ubiquitination and Proteolytic Processing of the p105 Precursor of Nuclear Factor κB1*
- Biology, ChemistryThe Journal of Biological Chemistry
- 1998
Interestingly, in the reconstituted system, the C-terminally truncated form of p 105, p97, was processed into p50 more efficiently than normal p105, even when both species were ubiquitinated to a similar extent, suggesting some additional mechanism involving theC-terminal region of p105 influences the proteolytic processing of the ubiquitination precursor.
MEKK1 activates both IκB kinase α and IκB kinase β
- Biology, Computer Science
- 1998
It is shown that recombinant IKK-α and Ikk-β can, in fact, directly phosphorylate IκBα at Ser-32 and Ser-36, as well as homologous residues in IKKBβ in vitro, and thus are bona fide IkkB kinases.
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