Phosphorylation of Arabidopsis Ubiquitin Ligase ATL31 Is Critical for Plant Carbon/Nitrogen Nutrient Balance Response and Controls the Stability of 14-3-3 Proteins

Yasuda, Shigetaka; Sato, Takeo; Maekawa, Shugo; Aoyama, Shigeyoshi; Fukao, Yoichiro; Yamaguchi, Junji

doi:10.1074/jbc.m113.533133

Cited by 64 publications

(59 citation statements)

References 61 publications

(70 reference statements)

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“…Given that ATL protein activity can be regulated by phosphorylation5051, we also evaluated the presence of putative phosphorylation sites using Musite. We thus identified at least one putative phosphorylation site in 69 of the 96 candidates, with a maximum of 16 putative phosphorylation sites identified in VviATL100 (Supplemental Table 1).…”

Section: Resultsmentioning

confidence: 99%

Genome-wide characterisation and expression profile of the grapevine ATL ubiquitin ligase family reveal biotic and abiotic stress-responsive and development-related members

Ariani

Regaiolo

Lovato

et al. 2016

Sci Rep

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The Arabidopsis Tóxicos en Levadura (ATL) protein family is a class of E3 ubiquitin ligases with a characteristic RING-H2 Zn-finger structure that mediates diverse physiological processes and stress responses in plants. We carried out a genome-wide survey of grapevine (Vitis vinifera L.) ATL genes and retrieved 96 sequences containing the canonical ATL RING-H2 domain. We analysed their genomic organisation, gene structure and evolution, protein domains and phylogenetic relationships. Clustering revealed several clades, as already reported in Arabidopsis thaliana and rice (Oryza sativa), with an expanded subgroup of grapevine-specific genes. Most of the grapevine ATL genes lacked introns and were scattered among the 19 chromosomes, with a high level of duplication retention. Expression profiling revealed that some ATL genes are expressed specifically during early or late development and may participate in the juvenile to mature plant transition, whereas others may play a role in pathogen and/or abiotic stress responses, making them key candidates for further functional analysis. Our data offer the first genome-wide overview and annotation of the grapevine ATL family, and provide a basis for investigating the roles of specific family members in grapevine physiology and stress responses, as well as potential biotechnological applications.

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Section: Resultsmentioning

confidence: 99%

Genome-wide characterisation and expression profile of the grapevine ATL ubiquitin ligase family reveal biotic and abiotic stress-responsive and development-related members

Ariani

Regaiolo

Lovato

et al. 2016

Sci Rep

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“…The 14-3-3 protein is a regulatory protein that interacts with the C-terminal part of AHA1 and phosphorylates AHA2 at a serine/threonine residue, thereby activating a PM H + -ATPase to generate a differential proton gradient across the guard cell membrane to open stomata (Jahn et al, 1997;Baunsgaard et al, 1998). The proteasome-mediated degradation of 14-3-3 proteins by the E3 ligase ATL31 has been shown to occur due to stress stimuli such as high-carbon or low-nitrogen conditions (Yasuda et al, 2014). Overexpression of RIN4 increases the activation of H + -ATPases, while the rin4 mutant has reduced H + -ATPase activity and is resistant to P. syringae pv tomato (DC3000) (Liu et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

GENERAL CONTROL NONREPRESSIBLE4 Degrades 14-3-3 and the RIN4 Complex to Regulate Stomatal Aperture with Implications on Nonhost Disease Resistance and Drought Tolerance

Kaundal

Vemanna

et al. 2017

Plant Cell

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“…Protein ubiquitination is likely to be initiated upon pollen activation in order to degrade the present proteins and to replace them with the newly synthesized species. Another E3 ubiquitin-protein ligase in Arabidopsis was reported to bind its target 14 -3-3-proteins only upon phosphorylation of its particular amino acids (70). If the E3 ligase identified in our data set acts also after phosphorylation, we might speculate that this phosphorylation event represents an activation phosphorylation.…”

Section: Discussionmentioning

confidence: 96%

Phosphoproteomics Profiling of Tobacco Mature Pollen and Pollen Activated in vitro

Fíla

Radau

Matros

et al. 2016

Molecular & Cellular Proteomics

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Tobacco mature pollen has extremely desiccated cytoplasm, and is metabolically quiescent. Upon re-hydration it becomes metabolically active and that results in later emergence of rapidly growing pollen tube. These changes in cytoplasm hydration and metabolic activity are accompanied by protein phosphorylation. In this study, we subjected mature pollen, 5-min-activated pollen, and 30-min-activated pollen to TCA/acetone protein extraction, trypsin digestion and phosphopeptide enrichment by titanium dioxide. The enriched fraction was subjected to nLC-MS/MS. We identified 471 phosphopeptides that carried 432 phosphorylation sites, position of which was exactly matched by mass spectrometry. These 471 phosphopeptides were assigned to 301 phosphoproteins, because some proteins carried more phosphorylation sites. Of the 13 functional groups, the majority of proteins were put into these categories: transcription, protein synthesis, protein destination and storage, and signal transduction. Many proteins were of unknown function, reflecting the fact that male gametophyte contains many specific proteins that have not been fully functionally annotated. The quantitative data highlighted the dynamics of protein phosphorylation during pollen activation; the identified phosphopeptides were divided into seven groups based on the regulatory trends. The major group comprised mature pollen-specific phosphopeptides that were dephosphorylated during pollen activation. Several phosphopeptides representing the same phosphoprotein had different regulation, which pinpointed the complexity of protein phosphorylation and its clear functional context. Collectively, we showed the first phosphoproteomics data on activated pollen where the position of phosphorylation sites was clearly demonstrated and regulatory kinetics was resolved. Molecular & Cellular

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Phosphorylation of Arabidopsis Ubiquitin Ligase ATL31 Is Critical for Plant Carbon/Nitrogen Nutrient Balance Response and Controls the Stability of 14-3-3 Proteins

Cited by 64 publications

References 61 publications

Genome-wide characterisation and expression profile of the grapevine ATL ubiquitin ligase family reveal biotic and abiotic stress-responsive and development-related members

Genome-wide characterisation and expression profile of the grapevine ATL ubiquitin ligase family reveal biotic and abiotic stress-responsive and development-related members

GENERAL CONTROL NONREPRESSIBLE4 Degrades 14-3-3 and the RIN4 Complex to Regulate Stomatal Aperture with Implications on Nonhost Disease Resistance and Drought Tolerance

Phosphoproteomics Profiling of Tobacco Mature Pollen and Pollen Activated in vitro

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