# 14-3-3 Proteins in Guard Cell Signaling

* Corresponding author
2 SAVE - Signalisation de l'Adaptation des Végétaux à l'Environnement
BIAM - Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) : DRF/BIAM
Abstract : Guard cells are specialized cells located at the leaf surface delimiting pores which control gas exchanges between the plant and the atmosphere. To optimize the CO$_2$ uptake necessary for photosynthesis while minimizing water loss, guard cells integrate environmental signals to adjust stomatal aperture. The size of the stomatal pore is regulated by movements of the guard cells driven by variations in their volume and turgor. As guard cells perceive and transduce a wide array of environmental cues, they provide an ideal system to elucidate early events of plant signaling. Reversible protein phosphorylation events are known to play a crucial role in the regulation of stomatal movements. However, in some cases, phosphorylation alone is not sufficient to achieve complete protein regulation, but is necessary to mediate the binding of interactors that modulate protein function. Among the phosphopeptide-binding proteins, the 14- 3-3 proteins are the best characterized in plants. The 14-3-3s are found as multiple isoforms in eukaryotes and have been shown to be involved in the regulation of stomatal movements. In this review, we describe the current knowledge about 14-3-3 roles in the regulation of their binding partners in guard cells: receptors, ion pumps, channels, protein kinases, and some of their substrates. Regulation of these targets by 14-3- 3 proteins is discussed and related to their function in guard cells during stomatal movements in response to abiotic or biotic stresses.
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Cited literature [133 references]

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Submitted on : Wednesday, June 26, 2019 - 11:47:28 AM
Last modification on : Monday, March 29, 2021 - 2:47:40 PM

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fpls-06-01210.pdf
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### Citation

Valérie Cotelle, Nathalie Leonhardt. 14-3-3 Proteins in Guard Cell Signaling. Frontiers in Plant Science, Frontiers, 2016, 6, pp.1210. ⟨10.3389/fpls.2015.01210⟩. ⟨cea-02165858⟩

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