Abstract:
:The transcriptional activity of NF-kappa B is stimulated upon phosphorylation of its p65 subunit on serine 276 by protein kinase A (PKA). The transcriptional coactivator CPB/p300 associates with NF-kappa B p65 through two sites, an N-terminal domain that interacts with the C-terminal region of unphosphorylated p65, and a second domain that only interacts with p65 phosphorylated on serine 276. Accessibility to both sites is blocked in unphosphorylated p65 through an intramolecular masking of the N terminus by the C-terminal region of p65. Phosphorylation by PKA both weakens the interaction between the N- and C-terminal regions of p65 and creates an additional site for interaction with CBP/p300. Therefore, PKA regulates the transcriptional activity of NF-kappa B by modulating its interaction with CBP/p300.
journal_name
Mol Celljournal_title
Molecular cellauthors
Zhong H,Voll RE,Ghosh Sdoi
10.1016/s1097-2765(00)80066-0subject
Has Abstractpub_date
1998-04-01 00:00:00pages
661-71issue
5eissn
1097-2765issn
1097-4164pii
S1097-2765(00)80066-0journal_volume
1pub_type
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