Posttranslational modification of the RHO of plants protein RACB by phosphorylation and cross-kingdom conserved ubiquitination

Small RHO-type G-proteins act as signaling hubs and master regulators of polarity in eukaryotic cells. Their activity is tightly controlled, as defective RHO signaling leads to aberrant growth and developmental defects. Two major processes regulate G-protein activity: canonical shuttling between dif...

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Vydáno v:	PloS one Ročník 17; číslo 3; s. e0258924
Hlavní autoři:	Weiß, Lukas, Gaelings, Lana, Reiner, Tina, Mergner, Julia, Kuster, Bernhard, Fehér, Attila, Hensel, Götz, Gahrtz, Manfred, Kumlehn, Jochen, Engelhardt, Stefan, Hückelhoven, Ralph
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	United States Public Library of Science 25.03.2022 Public Library of Science (PLoS)
Témata:	Amino acids Analysis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis thaliana Barley Binding proteins Biology and Life Sciences Comparative analysis Conservation Engineering and Technology Genetic aspects Hordeum - genetics Hordeum - metabolism Hordeum vulgare Humans Kinases Lipids Lysine Mass spectrometry Mutation Nucleotides Nucleotides - metabolism Oryza - genetics Oryza - metabolism Phosphorylation Physical Sciences Plant biology Plant Proteins - genetics Plant Proteins - metabolism Point mutation Polarity Post-translational modification Protein Processing, Post-Translational Proteins Proteomics Rac1 protein Ras genes Research and Analysis Methods Residues rho GTP-Binding Proteins - genetics rho GTP-Binding Proteins - metabolism Rho protein Scientific imaging Signaling Success Ubiquitination Germany
ISSN:	1932-6203, 1932-6203
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Shrnutí:	Small RHO-type G-proteins act as signaling hubs and master regulators of polarity in eukaryotic cells. Their activity is tightly controlled, as defective RHO signaling leads to aberrant growth and developmental defects. Two major processes regulate G-protein activity: canonical shuttling between different nucleotide bound states and posttranslational modification (PTM), of which the latter can support or suppress RHO signaling, depending on the individual PTM. In plants, regulation of Rho of plants (ROPs) signaling activity has been shown to act through nucleotide exchange and GTP hydrolysis, as well as through lipid modification, but there is little data available on phosphorylation or ubiquitination of ROPs. Hence, we applied proteomic analyses to identify PTMs of the barley ROP RACB. We observed in vitro phosphorylation by barley ROP binding kinase 1 and in vivo ubiquitination of RACB. Comparative analyses of the newly identified RACB phosphosites and human RHO protein phosphosites revealed conservation of modified amino acid residues, but no overlap of actual phosphorylation patterns. However, the identified RACB ubiquitination site is conserved in all ROPs from Hordeum vulgare , Arabidopsis thaliana and Oryza sativa and in mammalian Rac1 and Rac3. Point mutation of this ubiquitination site leads to stabilization of RACB. Hence, this highly conserved lysine residue may regulate protein stability across different kingdoms.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Current address: Chair of Brewing and Beverage Technology, Technical University of Munich (TUM), Freising, Germany Competing Interests: The authors have declared that no competing interests exist.
ISSN:	1932-6203 1932-6203
DOI:	10.1371/journal.pone.0258924