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Distinct B subunits of PP 2A regulate the NF ‐κB signalling pathway through dephosphorylation of IKK β, IκBα and RelA
Author(s) -
Tsuchiya Yoshihiro,
Osaki Keiko,
Kanamoto Mayu,
Nakao Yuki,
Takahashi Ena,
Higuchi Toru,
Kamata Hideaki
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12912
Subject(s) - dephosphorylation , trimer , protein subunit , phosphorylation , microbiology and biotechnology , iκb kinase , chemistry , iκbα , nf κb , signalling , signal transduction , dimer , biology , phosphatase , biochemistry , organic chemistry , gene
PP 2A is composed of a scaffolding subunit (A), a catalytic subunit (C) and a regulatory subunit (B) that is classified into four families including B, B′, B′′ and B′′′/striatin. Here, we found that a distinct PP 2A complex regulates NF ‐κB signalling by dephosphorylation of IKK β, IκBα and RelA/p65. The PP 2A core enzyme AC dimer and the holoenzyme AB ′′′C trimer dephosphorylate IKK β, IκBα and RelA, whereas the ABC trimer dephosphorylates IκBα but not IKK β and RelA in cells. In contrast, AB ′C and AB ′′C trimers have little effect on dephosphorylation of these signalling proteins. These results suggest that different forms of PP 2A regulate NF ‐κB pathway signalling through multiple steps each in a different manner, thereby finely tuning NF ‐κB‐ and IKK β‐mediated cellular responses.