Article
A dynamic charge-charge interaction modulates PP2A:B56 substrate recruitment.
eLife - 20 Mar 2020
Wang Xinru, Garvanska Dimitriya H, Nasa Isha, Ueki Yumi, Zhang Gang, Kettenbach Arminja N, Peti Wolfgang, Nilsson Jakob, Page Rebecca
Abstract excerpt
The recruitment of substrates by the ser/thr protein phosphatase 2A (PP2A) is poorly understood, limiting our understanding of PP2A-regulated signaling. Recently, the first PP2A:B56 consensus binding motif, LxxIxE, was identified. However, most validated LxxIxE motifs bind PP2A:B56 with micromolar affinities, suggesting that additional motifs exist to enhance PP2A:B56 binding. Here, we report the requirement of a...
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