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YODA-HSP90 module regulates phosphorylation-dependent inactivation of SPEECHLESS to control stomatal development under acute heat stress in Arabidopsis.

07:00 EST 11th January 2020 | BioPortfolio

Summary of "YODA-HSP90 module regulates phosphorylation-dependent inactivation of SPEECHLESS to control stomatal development under acute heat stress in Arabidopsis."

Stomatal ontogenesis, patterning, and function are hallmarks of environmental plant adaptation, especially to conditions limiting plant growth such as elevated temperatures and reduced water availability. The specification and distribution of a stomatal cell lineage and its terminal differentiation to guard cells requires a master regulatory protein phosphorylation cascade initiated by the YODA mitogen-activated protein kinase kinase kinase. YODA signaling results in the activation of MITOGEN-ACTIVATED PROTEIN KINASEs (MPK3 and MPK6), which confer regulation of transcription factors including SPEECHLESS (SPCH). Herein, we report that acute heat stress affects the phosphorylation and deactivation of SPCH and modulates stomatal density. By using complementary molecular, genetic, biochemical and cell biology approaches we provide solid evidence that HEAT SHOCK PROTEINS 90 (HSP90) play a crucial role in transducing heat-stress response through YODA cascade. Genetic studies revealed that YODA and HSP90.1 are epistatic, and they likely function linearly in the same developmental pathway regulating stomata formation. HSP90s interact with YODA, affect its cellular polarization, and modulate the phosphorylation of downstream targets, like MPK6 and SPCH, under both normal and heat-stress conditions. Thus, HSP90-mediated specification and differentiation of stomatal cell lineage couples stomatal development to environmental cues providing an adaptive mechanism to plant heat-stress response.

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Name: Molecular plant
ISSN: 1752-9867
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Medical and Biotech [MESH] Definitions

A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.

A group of enzymes that are dependent on cyclic GMP and catalyzes the phosphorylation of serine or threonine residues of proteins.

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A monomeric calcium-calmodulin-dependent protein kinase subtype that is primarily expressed in neuronal tissues; T-LYMPHOCYTES and TESTIS. The activity of this enzyme is regulated by its phosphorylation by CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASE KINASE.

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