Phosphorylation of NF-kappa B p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300.

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 Cell

journal_title

Molecular cell

authors

Zhong H,Voll RE,Ghosh S

doi

10.1016/s1097-2765(00)80066-0

subject

Has Abstract

pub_date

1998-04-01 00:00:00

pages

661-71

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)80066-0

journal_volume

1

pub_type

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