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

Yue, Kun, Sandal, Priyanka, Williams, Elisabeth L, Murphy, Evan, Stes, Elisabeth, Nikonorova, Natalia, Ramakrishna, Priya, Czyzewicz, Nathan, Montero-Morales, Laura, Kumpf, Robert, Lin, Zhefeng, van de Cotte, Brigitte, Iqbal, Mudassar, Van Bel, Michiel, Van De Slijke, Eveline, Meyer, Matthew R, Gadeyne, Astrid, Zipfel, Cyril, De Jaeger, Geert, Van Montagu, Marc, Van Damme, Daniël, Gevaert, Kris, Rao, A Gururaj, Beeckman, Tom and De Smet, Ive (2016) PP2A-3 interacts with ACR4 and regulates formative cell division in the Arabidopsis root. Proceedings of the National Academy of Sciences of the United States of America (PNAS), 113 (5). pp. 1447-1452. ISSN 1091-6490

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Abstract

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.

Item Type:	Article
Faculty \ School:	Faculty of Science > School of Biological Sciences
UEA Research Groups:	Faculty of Science > Research Groups > Plant Sciences
Depositing User:	Pure Connector
Date Deposited:	22 Apr 2016 08:33
Last Modified:	21 Oct 2022 04:32
URI:	https://ueaeprints.uea.ac.uk/id/eprint/58333
DOI:	10.1073/pnas.1525122113

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