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Wallace, I. S.

Publications and source records attributed to Wallace, I. S..

2 recordsLinked to original sources

Arabidopsis thaliana RHAMNOSE 1 condensate formation drives UDP-rhamnose synthesis

Rhamnose is an essential component of the plant cell wall and is synthesized from uridine diphosphate (UDP)-glucose by the RHAMNOSE1 (RHM1) enzyme. RHM1 localizes to biomolecular condensates in plants, but their identity, formation, and function remain elusive. Combining live imaging, genetics, and biochemical approaches in Arabidopsis and heterologous systems, we show that RHM1 alone is sufficient to form enzymatically active condensates, which we name rhamnosomes. Rhamnosome formation is required for UDP-rhamnose synthesis and organ development. Overall, our study demonstrates a novel role for biomolecular condensation in metabolism and organismal development, and provides further support for how organisms have harnessed this biophysical process to regulate small molecule metabolism. One-Sentence SummaryCondensation of RHM1 drives UDP-rhamnose synthesis during plant development.

plant biology↗

CALCIUM-DEPENDENT PROTEIN KINASE32 regulates cellulose biosynthesis through post-translational modification of cellulose synthase

Cellulose is an economically important source of food, paper, textiles, and biofuel. As an essential component of plant cell walls, cellulose is critical for plant cell growth. Despite its economic and biological significance, the regulation of cellulose biosynthesis is poorly understood. Phosphorylation and dephosphorylation of cellulose synthases (CESAs) were shown to impact the direction and velocity of cellulose synthase complexes (CSCs). Despite a high prevalence of phosphorylation sites in CESAs, the protein kinases that phosphorylate CESAs are largely unknown. Here, we demonstrate that CALCIUM-DEPENDENT PROTEIN KINASE32 (CPK32) regulates cellulose biosynthesis via phosphorylation of CESA3. Phosphorylation of CESA3 is important for the motility and stability of CSCs. Hence, we uncovered a new function of CPKs that regulates cellulose biosynthesis and a novel mechanism by which phosphorylation regulates the stability of CSCs.

plant biology↗