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Biology subjects

Grubb, L.

Publications and source records attributed to Grubb, L..

2 recordsLinked to original sources

Quantitative proteomics uncovers a role for REVEILLE8- like clock genes in osmotic and salt stress response in Arabidopsis

The plant circadian clock governs the precise regulation of plant developmental and environmental responses within a 24 h photoperiod. Consisting of a series of interconnected transcription factor moderated feedback loops, each operating at specific times of day within the photoperiod, more than 30% of Arabidopsis genes show circadian regulation. REVEILLE (RVE) genes exhibit highest expression in the afternoon, and act as activators of afternoon-expressed clock genes, including TOC1 and PRR5. Specifically, RVE4, 6 and 8 have been identified as regulators of both plant growth and development, along with temperature responses. Previous work using Arabidopsis has implicated soybean RVE8-like proteins in drought responses, however, there remains a lack of understanding of how these RVEs control abiotic stress responses, particularly relating to proteome-level regulation. Here, using quantitative proteomics, we resolve how the rve4 6 8 proteome responds to osmotic and salt stress at end-of-day and end-of-night timepoints. Our results indicate that rve4 6 8 plants have substantially altered regulation of proteins related to osmotic stress, photosynthesis and phenylpropanoid metabolism, particularly at end-of-day. Further, we resolve new drought-responsive targets impacted by the loss of RVE4, 6, and 8 that are involved in vesicle transport, fatty acid metabolism and abscission. Overall, our data provide a new resource for understanding how RVE8-like proteins impact plant drought-like responses, offering opportunities for future chronoculture-informed breeding of climate-resilient crops.

Plant Biology↗

Large-scale identification of ubiquitination sites on membrane-associated proteins in Arabidopsis thaliana seedlings

Protein phosphorylation and ubiquitination are two of the most abundant forms of post-translational modifications in eukaryotes, regulated by thousands of protein kinases, phosphatases, E3 ubiquitin ligases, and ubiquitin proteases. Although previous studies have catalogued several ubiquitinated proteins in plants (Walton et al., 2016), few membrane-localized proteins have been identified. Receptor kinases (RKs) initiate phosphorylation signal relays that regulate plant growth, development, and stress responses. While the regulatory role of phosphorylation on protein kinase function is well-documented (Couto and Zipfel, 2016), considerably less is known about the role of ubiquitination on protein kinase function, even though protein turnover is critical to their signaling competence and cellular homeostasis. Here we describe the large-scale identification of ubiquitination sites on Arabidopsis proteins associated with or integral to the plasma membrane, including over 100 protein kinases.

plant biology↗