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

Autor: Weiß L; Chair of Phytopathology, Technical University of Munich (TUM), Freising, Germany., Gaelings L; Chair of Phytopathology, Technical University of Munich (TUM), Freising, Germany., Reiner T; Chair of Phytopathology, Technical University of Munich (TUM), Freising, Germany., Mergner J; Chair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany., Kuster B; Chair of Proteomics and Bioanalytics, Technical University of Munich (TUM), Freising, Germany.; Bavarian Biomolecular Mass Spectrometry Center (BayBioMS), TUM, Freising, Germany., Fehér A; Chair of Plant Biology, University of Szeged, and Institute of Plant Biology, Biological Research Centre, Szeged, Hungary., Hensel G; Institute of Plant Genetics and Crop Plant Research (IPK), Gatersleben, Germany., Gahrtz M; Institute of Plant Genetics and Crop Plant Research (IPK), Gatersleben, Germany., Kumlehn J; Institute of Plant Genetics and Crop Plant Research (IPK), Gatersleben, Germany., Engelhardt S; Chair of Phytopathology, Technical University of Munich (TUM), Freising, Germany., Hückelhoven R; Chair of Phytopathology, Technical University of Munich (TUM), Freising, Germany.
Jazyk: angličtina
Zdroj: PloS one [PLoS One] 2022 Mar 25; Vol. 17 (3), pp. e0258924. Date of Electronic Publication: 2022 Mar 25 (Print Publication: 2022).
DOI: 10.1371/journal.pone.0258924
Abstrakt: 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.
Competing Interests: The authors have declared that no competing interests exist.
Databáze: MEDLINE
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