Back

A moss N-Acetyltransferase-MAPK protein controls 2D to 3D developmental transition via acetylation and phosphorylation changes

de Luxan Hernandez, C.; Ammitsoe, T. J.; Kanne, J. V.; Stanimirovic, S.; Roux, M.; Weeks, Z.; Schutzbier, M.; Dürnberger, G.; Roitinger, E.; Zhang, L.; Spadiut, O.; Ishikawa, M.; Hasebe, M.; Moody, L.; Dagdas, Y.; Rodriguez, E.; Petersen, M.

2025-05-03 plant biology
10.1101/2025.05.02.650421 bioRxiv
Show abstract

Post-translational modifications (PTMs) finetune plant responses to developmental and environmental cues by impacting protein activity, stability, localization and interaction landscape. In this study we identified a moss specific protein which combines two common PTMs: acetylation and phosphorylation. This protein originated from the fusion of a MAPK with an N-acetyltransferase, for which we named it Rosetta NATD-MAPK 1 (RAK1). Using biochemical methods, we demonstrated that RAK1 has acetyltransferase activity that is enhanced by activation of its MAPK domain. Phenotypical studies of rak1 knockout mutants revealed a role for RAK1 in the regulation of the 2D-to-3D growth transition. Through Mass Spectrometry we verified that defective 2D-to-3D transition in the mutants was caused by differentially regulated acetylation and phosphorylation events associated to metabolic reprogramming and 3D differentiation. Collectively, this study uncovers a previously unknown multidomain protein and provides insights into the interplay of PTMs during developmental reprogramming. TeaserAcetylation and phosphorylation changes modulate the 2D to 3D developmental transition in Physcomitrium patens.

Matching journals

The top 12 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.