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The structure of the PP2A regulatory subunit B56γ: The remaining piece of the PP2A jigsaw puzzle
Author(s) -
Magnusdottir Audur,
Stenmark Pål,
Flodin Susanne,
Nyman Tomas,
Kotenyova Tetyana,
Gräslund Susanne,
Ogg Derek,
Nordlund Pär
Publication year - 2009
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22150
Subject(s) - protein subunit , protein phosphatase 2 , dimer , heterotrimeric g protein , chemistry , specificity factor , serine , microbiology and biotechnology , stereochemistry , biochemistry , biophysics , enzyme , biology , g protein , gene , signal transduction , organic chemistry , rna dependent rna polymerase , polymerase
The PP2A serine/threonine phosphatase regulates a plethora of cellular processes. In the cell the predominant form of the enzyme is a heterotrimer, formed by a core dimer composed of a catalytic and a scaffolding subunit, which assemble together with one of a range of different regulatory B subunits. Here, we present the first structure of a free non‐complexed B subunit, B56γ. Comparison with the recent structures of a heterotrimeric complex and the core dimer reveals several significant conformational changes in the interface region between the B56γ and the core dimer. These allow for an assembly scheme of the PP2A holoenzyme to be put forth where B56γ first complexes with the scaffolding subunit and subsequently binds to the catalytic subunit and this induces the formation of a binding site for the invariant C‐terminus of the catalytic subunit that locks in the complex as a last step of assembly. Proteins 2009. © 2008 Wiley‐Liss, Inc.