The Arabidopsis F-box protein AtFBS1 interacts with 14-3-3 proteins

Sepúlveda-García, Edgar; Rocha-Sosa, Mario

doi:10.1016/j.plantsci.2012.06.009

Cited by 11 publications

(38 citation statements)

References 52 publications

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“…FBS1 interacts with Arabidopsis Skp1 (ASK1) by yeast two-hybrid assays, indicating that it forms a canonical SCF complex capable of labeling proteins for degradation [68]. Understanding then exactly how FBS1 accomplishes its regulatory effects, and why it appears to regulate only a subset of JA biosynthesis genes, will likely come from identifying its ubiquitylation target(s).…”

Section: Discussionmentioning

confidence: 99%

“…It may be that this subset is supposed to selectively respond to abiotic stresses through FBS1 action stimulated by particular environmental conditions. FBS1 also interacts with five of 13 14–3-3 proteins encoded by the Arabidopsis genome in yeast two-hybrid or pull down assays [68]. Intriguingly, three of these FBS1 14–3-3 interactors have recently been shown to negatively regulate plant responses to cold and salt [70–72].…”

Section: Discussionmentioning

confidence: 99%

“…Intriguingly, three of these FBS1 14–3-3 interactors have recently been shown to negatively regulate plant responses to cold and salt [70–72]. However, functional and mechanistic links between these 14–3-3 proteins and FBS1 are not established, and preliminary findings suggest that 14–3-3 proteins might not be SCF FBS1 ubiquitylation targets [68]. …”

Section: Discussionmentioning

confidence: 99%

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Transcriptome analysis uncovers Arabidopsis F-BOX STRESS INDUCED 1 as a regulator of jasmonic acid and abscisic acid stress gene expression

et al. 2017

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BackgroundThe ubiquitin 26S proteasome system (UPS) selectively degrades cellular proteins, which results in physiological changes to eukaryotic cells. F-box proteins are substrate adaptors within the UPS and are responsible for the diversity of potential protein targets. Plant genomes are enriched in F-box genes, but the vast majority of these have unknown roles. This work investigated the Arabidopsis F-box gene F-BOX STRESS INDUCED 1 (FBS1) for its effects on gene expression in order elucidate its previously unknown biological function.ResultsUsing publically available Affymetrix ATH1 microarray data, we show that FBS1 is significantly co-expressed in abiotic stresses with other well-characterized stress response genes, including important stress-related transcriptional regulators. This gene suite is most highly expressed in roots under cold and salt stresses. Transcriptome analysis of fbs1–1 knock-out plants grown at a chilling temperature shows that hundreds of genes require FBS1 for appropriate expression, and that these genes are enriched in those having roles in both abiotic and biotic stress responses. Based on both this genome-wide expression data set and quantitative real-time PCR (qPCR) analysis, it is apparent that FBS1 is required for elevated expression of many jasmonic acid (JA) genes that have established roles in combatting environmental stresses, and that it also controls a subset of JA biosynthesis genes. FBS1 also significantly impacts abscisic acid (ABA) regulated genes, but this interaction is more complex, as FBS1 has both positive and negative effects on ABA-inducible and ABA-repressible gene modules. One noteworthy effect of FBS1 on ABA-related stress processes, however, is the restraint it imposes on the expression of multiple class I LIPID TRANSFER PROTEIN (LTP) gene family members that have demonstrated protective effects in water deficit-related stresses.Conclusion FBS1 impacts plant stress responses by regulating hundreds of genes that respond to the plant stress hormones JA and ABA. The positive effect that FBS1 has on JA processes and the negative effect it has on at least some ABA processes indicates that it in part regulates cellular responses balanced between these two important stress hormones. More broadly then, FBS1 may aid plant cells in switching between certain biotic (JA) and abiotic (ABA) stress responses. Finally, because FBS1 regulates a subset of JA biosynthesis and response genes, we conclude that it might have a role in tuning hormone responses to particular circumstances at the transcriptional level.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-017-3864-6) contains supplementary material, which is available to authorized users.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Transcriptome analysis uncovers Arabidopsis F-BOX STRESS INDUCED 1 as a regulator of jasmonic acid and abscisic acid stress gene expression

et al. 2017

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“…The role of 14-3-3 proteins in protein degradation through ubiquitin E3 protein ligases has been reported in Arabidopsis . A stress-responsive F-box protein, FBS1, has been shown to interact with 14-3-3 proteins, and this interaction is important for FBS1 degradation by the 26S proteasome [ 45 ]. 14-3-3 proteins also interact with components of an E3 ligase, ETO1/ELOs, and promote their degradation in ethylene biosynthesis [ 46 ], suggesting that regulation of protein degradation by 14-3-3 proteins may be a general mechanism in plants.…”

Section: Discussionmentioning

confidence: 99%

14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs

Adams

Diaz

Hong

et al. 2014

IJMS

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14-3-3 proteins are regulatory proteins found in all eukaryotes and are known to selectively interact with phosphorylated proteins to regulate physiological processes. Through an affinity purification screening, many light-related proteins were recovered as 14-3-3 candidate binding partners. Yeast two-hybrid analysis revealed that the 14-3-3 kappa isoform (14-3-3κ) could bind to PHYTOCHROME INTERACTING FACTOR3 (PIF3) and CONSTITUTIVE PHOTOMORPHOGENIC1 (COP1). Further analysis by in vitro pull-down assay confirmed the interaction between 14-3-3κ and PIF3. Interruption of putative phosphorylation sites on the 14-3-3 binding motifs of PIF3 was not sufficient to inhibit 14-3-3κ from binding or to disturb nuclear localization of PIF3. It was also indicated that 14-3-3κ could bind to other members of the PIF family, such as PIF1 and PIF6, but not to LONG HYPOCOTYL IN FAR-RED1 (HFR1). 14-3-3 mutants, as well as the PIF3 overexpressor, displayed longer hypocotyls, and a pif3 mutant displayed shorter hypocotyls than the wild-type in red light, suggesting that 14-3-3 proteins are positive regulators of photomorphogenesis and function antagonistically with PIF3. Consequently, our results indicate that 14-3-3 proteins bind to PIFs and initiate photomorphogenesis in response to a light signal.

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“…Thus, across kingdoms, atypical FBX proteins with an N-terminal protein interaction domain, in addition to a C-terminal targeting domain, achieve expanded function by having further regulatory capacity and/or coordinating multiple cellular outputs through a dual targeting structure. F-BOX STRESS INDUCED (FBS) proteins are a far less understood subfamily of four plant FBX proteins with atypical structure (Maldonado-Calderon et al, 2012;Sepulveda-Garcia and Rocha-Sosa, 2012;Gonzalez et al, 2017). FBS1 is the founding member of this FBX subfamily and is recognized for its broad biotic and abiotic stress responsive gene induction profiles (Maldonado-Calderon et al, 2012;Gonzalez et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

A WD40 repeat-like protein pathway connects F-BOX STRESS INDUCED (FBS) proteins to the NIGT1.1 transcriptional repressor in Arabidopsis

Sepúlveda-García

Fulton

Parlan

et al. 2020

Preprint

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SCF-type E3 ubiquitin ligases use F-box (FBX) proteins as interchangeable substrate adaptors to recruit protein targets for ubiquitylation. FBX proteins almost universally have structure with two domains. A conserved N-terminal F-box domain interacts with a SKP protein and connects the FBX protein to the core SCF complex, while a C-terminal domain interacts with the protein target and facilitates recruitment. The F-BOX STRESS INDUCED (FBS) subfamily of four plant FBX proteins has atypical domain structure, however, with a centrally located F-box domain and additional conserved regions at both the N- and C-termini. FBS proteins have been linked to environmental stress networks, but no ubiquitylation target(s) or exact biological function has been established for this subfamily. We have identified two WD40 repeat-like proteins in Arabidopsis that are highly conserved in plants and interact with FBS proteins, which we have named FBS INTERACTING PROTEINs (FBIPs). FBIPs interact exclusively with the N-terminus of FBS proteins, and this interaction occurs in the nucleus. FBS1 destabilizes FBIP1, consistent with FBIPs being ubiquitylation targets of SCFFBS complexes. Furthermore, we found that FBIP1 interacts with NIGT1.1, a GARP-type transcriptional repressor that regulates nitrate and phosphate starvation signaling and responses. Collectively, these interactions between FBS, FBIP, and NIGT1.1 proteins delineate a previously unrecognized SCF-connected transcription regulation module that works in the context of phosphate and nitrate starvation, and possibly other environmental stresses. Importantly, this work also identified two uncharacterized WD40 repeat-like proteins as new tools with which to probe how an atypical SCF complex, SCFFBS, functions via FBX protein N-terminal interaction events.

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The Arabidopsis F-box protein AtFBS1 interacts with 14-3-3 proteins

Cited by 11 publications

References 52 publications

Transcriptome analysis uncovers Arabidopsis F-BOX STRESS INDUCED 1 as a regulator of jasmonic acid and abscisic acid stress gene expression

Transcriptome analysis uncovers Arabidopsis F-BOX STRESS INDUCED 1 as a regulator of jasmonic acid and abscisic acid stress gene expression

14-3-3 Proteins Participate in Light Signaling through Association with PHYTOCHROME INTERACTING FACTORs

A WD40 repeat-like protein pathway connects F-BOX STRESS INDUCED (FBS) proteins to the NIGT1.1 transcriptional repressor in Arabidopsis

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