PP2A-3 interacts with ACR4 and regulates formative cell division in the Arabidopsis root

Kun Yue, Priyanka Sandal, Elisabeth L Williams, Evan Murphy, Elisabeth Stes, Natalia Nikonorova, Priya Ramakrishna, Nathan Czyzewicz, Laura Montero-Morales, Robert Kumpf, Zhefeng Lin, Brigitte van de Cotte, Mudassar Iqbal, Michiel Van Bel, Eveline Van De Slijke, Matthew R Meyer, Astrid Gadeyne, Cyril Zipfel, Geert De Jaeger, Marc Van MontaguDaniël Van Damme, Kris Gevaert, A Gururaj Rao, Tom Beeckman, Ive De Smet

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In plants, the generation of new cell types and tissues depends on coordinated and oriented formative cell divisions. The plasma membrane-localized receptor kinase ARABIDOPSIS CRINKLY 4 (ACR4) is part of a mechanism controlling formative cell divisions in the Arabidopsis root. Despite its important role in plant development, very little is known about the molecular mechanism with which ACR4 is affiliated and its network of interactions. Here, we used various complementary proteomic approaches to identify ACR4-interacting protein candidates that are likely regulators of formative cell divisions and that could pave the way to unraveling the molecular basis behind ACR4-mediated signaling. We identified PROTEIN PHOSPHATASE 2A-3 (PP2A-3), a catalytic subunit of PP2A holoenzymes, as a previously unidentified regulator of formative cell divisions and as one of the first described substrates of ACR4. Our in vitro data argue for the existence of a tight posttranslational regulation in the associated biochemical network through reciprocal regulation between ACR4 and PP2A-3 at the phosphorylation level.

Original languageEnglish
Pages (from-to)1447-1452
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America (PNAS)
Issue number5
Publication statusPublished - 2 Feb 2016

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