ArticleNature plants2026
Evolutionary tuning of the molecular charge state of UBP24 shapes responses to high temperature.
Article in Nature plants, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Protein evolution is shaped by sequence variation that modulates protein properties-for example, through the gain or loss of post-translational modifications. Among these, reversible phosphorylation alters a protein's overall electrical charge and enables organisms to dynamically respond to environmental fluctuations. In plants, the hydro-active opening of stomata, microscopic pores that regulate gas exchange and leaf temperature, is governed by phosphorylation-dependent signalling. Here we identify a mechanism involving the deubiquitylase UBIQUITIN-SPECIFIC PROTEASE 24 (UBP24) that promotes stomatal opening in Arabidopsis thaliana under heat. UBP24 is phosphorylated at serine 360 by the kinase OPEN STOMATA 1, which is activated by B4 RAF kinases in response to heat stress. This phosphorylation stabilizes UBP24, enabling the deubiquitylation of a plasma membrane H
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