F-box proteins everywhere

Lechner, Esther; Achard, Patrick; Vansiri, Amérin; Potuschak, Thomas; Genschik, Pascal

doi:10.1016/j.pbi.2006.09.003

Cited by 332 publications

(297 citation statements)

References 68 publications

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“…This observation is consistent with a recent systems biology study exploring the Arabidopsis interactome, wherein both KFB01 and KFB50 were found to potentially interact with the PAL enzymes (Arabidopsis Interactome Mapping Consortium, 2011). Each of the three KFB proteins contains a highly conserved F-box motif at the N terminus, which interacts with the SKP1 subunit of the E3 ligase complex (Lechner et al, 2006), and two or three putative Kelch motifs at the C terminus (Figure 1). Subsequently, we amplified the full-length cDNAs of the three KFB proteins and four PAL isoforms and revalidated their pairwise interactions in Y2H assays (Figure 1).…”

Section: Pal Isozymes Physically Interact With Kfb Proteins In Vitro mentioning

confidence: 99%

“…Ubiquitin conjugation requires the sequential action of three enzyme complexes: the ubiquitin-activating enzyme (E1), the ubiquitin-conjugating enzyme (E2), and the ubiquitin-protein ligase (E3). Members of the Skp1-Cullin-F-box (SCF) complex class of E3 ligases generally comprise four main subunits: SKP1, Cullin1, RBX1, and one member of the large family of F-box proteins (del Pozo and Estelle, 2000; Lechner et al, 2006). Within this complex, cullin interacts both with SKP1 and RBX1, forming a scaffold on which different F-box proteins assemble.…”

Section: Introductionmentioning

confidence: 99%

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Arabidopsis Kelch Repeat F-Box Proteins Regulate Phenylpropanoid Biosynthesis via Controlling the Turnover of Phenylalanine Ammonia-Lyase

2013

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Phenylalanine ammonia-lyase (PAL) catalyzes the first rate-limiting step in the phenylpropanoid pathway, which controls carbon flux to a variety of bioactive small-molecule aromatic compounds, and to lignin, the structural component of the cell wall. PAL is regulated at both the transcriptional and translational levels. Our knowledge about the transcriptional regulation of PAL is relatively comprehensive, but our knowledge of the molecular basis of the posttranslational regulation of PAL remains limited. Here, we demonstrate that the Arabidopsis thaliana Kelch repeat F-box (KFB) proteins KFB01, KFB20, and KFB50 physically interact with four PAL isozymes and mediate their proteolytic turnover via the ubiquitination-26S proteasome pathway. The KFB genes are differentially expressed in Arabidopsis tissues and respond to developmental and environmental cues. Up-or downregulation of their expression reciprocally affects the stability of the PAL enzymes, consequently altering the levels of phenylpropanoids. These data suggest that the KFB-mediated protein ubiquitination and degradation regulates the proteolysis of PALs, thus posttranslationally regulating phenylpropanoid metabolism. Characterizing the KFB-mediated proteolysis of PAL enzymes may inform future strategies for manipulating the synthesis of bioactive phenolics.

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Section: Pal Isozymes Physically Interact With Kfb Proteins In Vitro mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Arabidopsis Kelch Repeat F-Box Proteins Regulate Phenylpropanoid Biosynthesis via Controlling the Turnover of Phenylalanine Ammonia-Lyase

2013

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“…ETP1 and ETP2 belong to a novel subfamily of F-box protein of which little is known (Gagne et al 2002). Specifically, both ETP1 and ETP2 carry the F-box protein-associated (FBA_1) motif, which is different from typical proteinprotein interaction domains carried by most well-known F-box proteins (Lechner et al 2006). We found that the nontypical FBA_1 domain interacts directly with EIN2, indicating that this region may play a role in recognition of its substrates, which in our case is EIN2 (data not shown).…”

Section: Ein2 C-terminal End Is Of Crucial Importance To Ethylene Resmentioning

confidence: 99%

Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of EIN2 triggers ethylene responses in Arabidopsis

et al. 2009

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The gaseous plant hormone ethylene can trigger myriad physiological and morphological responses in plants. While many ethylene signaling pathway components have been identified and characterized, little is known about the function of the integral membrane protein ETHYLENE-INSENSITIVE2 (EIN2), a central regulator of all ethylene responses. Here, we demonstrate that Arabidopsis thaliana EIN2 is a protein with a short half-life that undergoes rapid proteasome-mediated protein turnover. Moreover, EIN2 protein accumulation is positively regulated by ethylene. We identified two F-box proteins, EIN2 TARGETING PROTEIN1 (ETP1) and EIN2 TARGETING PROTEIN2 (ETP2), that interact with the EIN2 C-terminal domain (EIN2-CEND), which is highly conserved and sufficient to activate most ethylene responses. Overexpression of ETP1 or ETP2 disrupts EIN2 protein accumulation, and these plants manifest a strong ethylene-insensitive phenotype. Furthermore, knocking down the levels of both ETP1 and ETP2 mRNAs using an artificial microRNA (amiRNA) leads to accumulation of EIN2 protein, resulting in plants that display constitutive ethylene response phenotypes. Finally, ethylene downregulates ETP1 and ETP2 proteins, impairing their ability to interact with EIN2. Thus, these studies reveal that a complex interplay between ethylene, the regulation of ETP1/ETP2 F-box proteins, and subsequent targeting and degradation of EIN2 is essential for triggering ethylene responses in plants.[Keywords: Hormone; protein degradation; signal transduction; plant] Supplemental material is available at http://www.genesdev.org.

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“…The F-box protein ORE9 has been suggested to be a positive regulator of leaf senescence, because mutants lacking ORE9 expression are delayed in senescence (Woo et al, 2001). Generally, F-box proteins are part of SCF-type E3 complexes with ubiquitin ligase activity and recruit target substrates to such complexes (Lechner et al, 2006). It has recently been shown that ORE9 indeed interacts with the core SCF subunits ARABIDOPSIS SKP1 HOMOLOGUE1 and CULLIN1 in planta (Stirnberg et al, 2007).…”

mentioning

confidence: 99%

Early Senescence and Cell Death in Arabidopsis saul1 Mutants Involves the PAD4-Dependent Salicylic Acid Pathway

Vogelmann

Drechsel²,

Bergler³

et al. 2012

Plant Physiology

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Age-dependent leaf senescence and cell death in Arabidopsis (Arabidopsis thaliana) requires activation of the transcription factor ORESARA1 (ORE1) and is not initiated prior to a leaf age of 28 d. Here, we investigate the conditional execution of events that regulate early senescence and cell death in senescence-associated ubiquitin ligase1 (saul1) mutants, deficient in the PLANT U-BOX-ARMADILLO E3 ubiquitin ligase SAUL1. In saul1 mutants challenged with low light, the switch of age-dependent cell death was turned on prematurely, as indicated by the accumulation of ORE1 transcripts, induction of the senescence marker gene SENESCENCE-ASSOCIATED GENE12, and cell death. However, ORE1 accumulation by itself was not sufficient to cause saul1 phenotypes, as demonstrated by double mutant analysis. Exposure of saul1 mutants to low light for only 24 h did not result in visible symptoms of senescence; however, the senescence-promoting transcription factor genes WRKY53, WRKY6, and NAC-LIKE ACTIVATED BY AP3/PI were up-regulated, indicating that senescence in saul1 seedlings was already initiated. To resolve the time course of gene expression, microarray experiments were performed at narrow intervals. Differential expression of the genes involved in salicylic acid and defense mechanisms were the earliest events detected, suggesting a central role for salicylic acid in saul1 senescence and cell death. The salicylic acid content increased in low-light-treated saul1 mutants, and application of exogenous salicylic acid was indeed sufficient to trigger saul1 senescence in permissive light conditions. Double mutant analyses showed that PHYTOALEXIN DEFICIENT4 (PAD4) but not NONEXPRESSER OF PR GENES1 (NPR1) is essential for saul1 phenotypes. Our results indicate that saul1 senescence depends on the PAD4-dependent salicylic acid pathway but does not require NPR1 signaling.

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F-box proteins everywhere

Cited by 332 publications

References 68 publications

Arabidopsis Kelch Repeat F-Box Proteins Regulate Phenylpropanoid Biosynthesis via Controlling the Turnover of Phenylalanine Ammonia-Lyase

Arabidopsis Kelch Repeat F-Box Proteins Regulate Phenylpropanoid Biosynthesis via Controlling the Turnover of Phenylalanine Ammonia-Lyase

Interplay between ethylene, ETP1/ETP2 F-box proteins, and degradation of EIN2 triggers ethylene responses in Arabidopsis

Early Senescence and Cell Death in Arabidopsis saul1 Mutants Involves the PAD4-Dependent Salicylic Acid Pathway

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