ArticlebioRxiv : the preprint server for biology2026
Phosphovariants of the canonical heterotrimeric Gα protein, GPA1, differentially affect G protein activity and Arabidopsis development.
Article in bioRxiv : the preprint server for biology, 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
Heterotrimeric G protein signaling downstream of receptor-like kinases (RLKs) is an emerging and important signal transduction mechanism in plants. However, little is known about the effects of phosphorylation events on the function of the canonical Gα subunit, GPA1. That several known phosphosites reside within important nucleotide co-factor binding sites suggests a role of phosphorylation in modulating the GTP/GDP binding and hydrolysis cycle of GPA1. To mimic and assess the effects of GPA1 phosphorylation, we created ten different phosphovariants of GPA1 and then comprehensively measured
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