ArticleMolecular and cellular biology1996
Basal phosphorylation of the PEST domain in the I(kappa)B(beta) regulates its functional interaction with the c-rel proto-oncogene product.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 84 citations in OpenAlex.
- CD5 dynamically calibrates basal NF-κB signaling in T cells during thymic development and peripheral activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Prediction of the presence of a seventh ankyrin repeat in IκBε from homology modeling combined with hydrogen-deuterium exchange mass spectrometry (HDX-MS).Protein science : a publication of the Protein Society · 2018Article
- Therapeutic targeting of CK2 in acute and chronic leukemias.Leukemia · 2018Review
- Overexpression of Hypo-Phosphorylated IκBβ at Ser313 Protects the Heart against Sepsis.PloS one · 2016Article
- Inhibiting IκBβ-NFκB signaling attenuates the expression of select pro-inflammatory genes.Journal of cell science · 2015Article
- Fas-associated factor (Faf1) is a novel CD40 interactor that regulates CD40-induced NF-κB activation via a negative feedback loop.Cell death & disease · 2014Article
- Article
- Alternative nuclear functions for NF-κB family members.American journal of cancer research · 2011Article
- IkappaBbeta acts to inhibit and activate gene expression during the inflammatory response.Nature · 2010Article
- Specification of DNA binding activity of NF-kappaB proteins.Cold Spring Harbor perspectives in biology · 2009Review
- Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway.Oncogene · 2006Review
- A comprehensive map of the toll-like receptor signaling network.Molecular systems biology · 2006Review
- Mitochondria to nucleus stress signaling: a distinctive mechanism of NFkappaB/Rel activation through calcineurin-mediated inactivation of IkappaBbeta.The Journal of cell biology · 2003Article
- Acetylation of RelA at discrete sites regulates distinct nuclear functions of NF-kappaB.The EMBO journal · 2002Article
- Molecular mechanisms in lymphocyte activation and growth.Immunologic research · 2001Review
- Inhibition of IkappaB kinase and IkappaB phosphorylation by 15-deoxy-Delta(12,14)-prostaglandin J(2) in activated murine macrophages.Molecular and cellular biology · 2000Article
- Mechanisms by which IkappaB proteins control NF-kappaB activity.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Functional redundancy of the nuclear factor kappa B inhibitors I kappa B alpha and I kappa B beta.The Journal of experimental medicine · 1998Article
- Regulation of serum amyloid A protein expression during the acute-phase response.The Biochemical journal · 1998Review
- DNA-dependent protein kinase phosphorylation of IkappaB alpha and IkappaB beta regulates NF-kappaB DNA binding properties.Molecular and cellular biology · 1998Article
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5 authors at 2 institutions in 1 country.
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Abstract
The product of the c-rel proto-oncogene (c-Rel) belongs to the NF-kappaB/Rel family of polypeptides and has been implicated in the transcriptional control of cell proliferation and immune function. In human T lymphocytes, c-Rel is sequestered in the cytoplasmic compartment by constitutively phosphorylated inhibitors, including I(kappa)B(alpha) and I(kappa)B(beta). Studies with bacterially expressed forms of these inhibitory proteins revealed that unphosphorylated I(kappa)B(alpha) but not I(kappa)B(beta) assembles with c-Rel and inhibits its DNA binding activity. Furthermore, latent I(kappa)B(beta)-c-Rel complexes derived from mammalian cells were sensitive to phosphatase treatment, whereas I(kappa)B(alpha)-c-Rel complexes were resistant. We have identified a constitutive protein kinase in unstimulated T cells that associates with and phosphorylates I(kappa)B(beta) in vitro. The substrate specificity, electrophoretic mobility, and antigenic properties of this I(kappa)B(beta)-associated kinase (BAK) suggest identity with casein kinase II (CKII), an enzyme known to mediate basal phosphorylation of I(kappa)B(alpha). Phosphorylation of recombinant I(kappa)B(beta) by either BAK or CKII restored the capacity of this inhibitor to antagonize the DNA binding activity of c-Rel. Peptide mapping and mutational analyses localized the bulk of the basal phosphorylation sites in I(kappa)B(beta) to the C-terminal PEST domain, which contains two potential acceptors for CKII-mediated phosphoryl group transfer (Ser-313 and Ser-315). Point mutations introduced into the full-length inhibitor at Ser-313 and Ser-315 led to a significant reduction in the phosphorylation of I(kappa)B(beta) and severely impaired its c-Rel inhibitory function in vivo. Taken together, these findings strongly suggest that basal phosphorylation of the PEST domain of I(kappa)B(beta) at consensus CKII sites is required for the efficient formation of latent I(kappa)B(beta)-c-Rel complexes.
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