Uma Kota

TL;DR: A sequential transphosphorylation model in which BRI1 controls signaling specificity by direct BR binding followed by substrate phosphorylation is proposed, which suggests both conservation and distinct differences between the molecular mechanisms regulating phosphorylated-dependent kinase activation in plant and animal receptor kinases.

TL;DR: It is reported that recombinant cytoplasmic domains of BRI1 and BAK1 also autophosphorylate on tyrosine residues and thus are dual-specificity kinases, suggesting that tyosine signaling should be considered with other plant receptor kinases as well.

TL;DR: In vitro analysis of AtPI4Kgamma4 indicates that it interacts directly with, and phosphorylates, two proteins involved in the ubiquitin-proteasome system, namely UFD1 (ubiquitin fusion degradation 1) and RPN10 (regulatory particle non-ATPase 10).

TL;DR: In this article, the authors present the latest advancements developed for the isolation and fractionation of plant organelles and their membrane components amenable to mass spectrometry (MS) analysis.

TL;DR: This study employed high-throughput cloning and a variety of mass spectrometry approaches to generate an autophosphorylation site database representative of more than 30% of the approximately 223 LRR RLKs in Arabidopsis thaliana, and used this database to analyze trends in the localization of phosphorylation sites across cytoplasmic kinase subdomains.