Lessons from Fungal F-Box Proteins

Jonkers, Wilfried; Rep, Martijn

doi:10.1128/ec.00386-08

Cited by 81 publications

(93 citation statements)

References 218 publications

(194 reference statements)

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“…Recently, we have demonstrated that Mdm30, an F-box protein, is also involved in stimulation of nuclear export of mRNA in yeast Shukla et al 2009). An F-box is a conserved protein motif of ∼50 amino acids (Bai et al 1994(Bai et al , 1996Jonkers and Rep 2009) and functions as a component of SCF (Skp1-Cul1-F-box-protein) ubiquitin ligase complex to facilitate the interaction between substrate and ubiquitin conjugating enzyme for covalent transfer of ubiquitin onto substrate (Bai et al 1996;Skowyra et al 1997;Reed 2003;Yen and Elledge 2008;Jonkers and Rep 2009). Like other F-box proteins, Mdm30 copurifies with SCF components (Uetz et al 2000;Kus et al 2004;Cohen et al 2008;Lackner and Nunnari 2009) and is involved in ubiquitylation and proteasomal degradation of Fzo1 and Mdm34 for the maintenance of fusion competent mitochondria (Fritz et al 2003;Meeusen and Nunnari 2005;Cohen et al 2008;Ota et al 2008;Livnat-Levanon and Glickman 2011).…”

Section: Introductionmentioning

confidence: 99%

A new regulatory pathway of mRNA export by an F-box protein, Mdm30

Durairaj¹,

Lahudkar²,

Bhaumik³

2013

RNA

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Mdm30, an F-box protein in yeast, has been recently shown to promote mRNA export. However, it remains unknown how Mdm30 facilitates mRNA export. Here, we show that Mdm30 targets the Sub2 component of the TREX (Transcription/Export) complex for ubiquitylation and subsequent proteasomal degradation. Such a targeted degradation of Sub2 enhances the recruitment of the mRNA export adaptor, Yra1, to the active genes to promote mRNA export. Together, these results elucidate that Mdm30 promotes mRNA export by lowering Sub2's stability and consequently enhancing Yra1 recruitment, thus illuminating new regulatory mechanisms of mRNA export by Mdm30.

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Section: Introductionmentioning

confidence: 99%

A new regulatory pathway of mRNA export by an F-box protein, Mdm30

Durairaj¹,

Lahudkar²,

Bhaumik³

2013

RNA

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“…Fungal SCF complexes have been reported to regulate a variety of cellular functions (17). Our previous studies identified an Fbox protein, Fbp1, that is essential for fungal virulence despite its dispensability for the development of several classical virulence factors, including the production of melanin, capsule formation, and growth at 37°C (21).…”

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confidence: 99%

The Casein Kinase I Protein Cck1 Regulates Multiple Signaling Pathways and Is Essential for Cell Integrity and Fungal Virulence in Cryptococcus neoformans

Wang

Liu²,

Patel³

et al. 2011

Eukaryot Cell

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Casein kinases regulate a wide range of cellular functions in eukaryotes, including phosphorylation of proteins that are substrates for degradation via the ubiquitin-proteasome system (UPS). Our previous study demonstrated that Fbp1, a component of the SCF FBP1 E3 ligase complex, was essential for Cryptococcus virulence. Because the Saccharomyces cerevisiae homolog of Fbp1, Grr1, requires casein kinase I (Yck1 and Yck2) to phosphorylate its substrates, we investigated the function of casein kinase I in Cryptococcus neoformans. In this report, we identified a C. neoformans casein kinase I protein homolog, Cck1. Similar to Fbp1, the expression of Cck1 is negatively regulated by glucose and during mating. cck1 null mutants showed significant virulence attenuation in a murine systemic infection model, but Cck1 was dispensable for the development of classical virulence factors (capsule, melanin, and growth at 37°C). cck1 mutants were hypersensitive to SDS treatment, indicating that Cck1 is required for cell integrity. The functional overlap between Cck1 and Fbp1 suggests that Cck1 may be required for the phosphorylation of Fbp1 substrates. Interestingly, the cck1 mutant also showed increased sensitivity to osmotic stress and oxidative stress, suggesting that Cck1 regulates both cell integrity and the cellular stress response. Our results show that Cck1 regulates the phosphorylation of both Mpk1 and Hog1 mitogen-activated protein kinases (MAPKs), demonstrating that Cck1 regulates cell integrity via the Mpk1 pathway and regulates cell adaptation to stresses via the Hog1 pathway. Overall, our study revealed that Cck1 plays important roles in regulating multiple signaling pathways and is required for fungal pathogenicity.

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“…Lately, Kelch domain-containing F-box (KFB) proteins were shown to be involved in regulation of the phenylpropanoid pathway (Shao et al, 2012;Zhang et al, 2013Zhang et al, , 2015. F-box proteins serve as substrate recruitment domains in the S-phase kinaseassociated protein1, Cullin, F-box (SCF) E3 ubiquitin ligase complexes, targeting protein substrates to 26S proteasomedependent degradation, in which the F box serves as the target recognition factor, mediating the specificity of the complex (Jonkers and Rep, 2009). In plants, the F-box superfamily seems to have gone through vast duplication and specialization.…”

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confidence: 99%

A Kelch domain-containing F-box coding gene negatively regulates flavonoid accumulation in Cucumis melo L.

Feder

Burger²,

Gao

et al. 2015

Plant Physiol.

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The flavonoids are phenylpropanoid-derived metabolites that are ubiquitous in plants, playing many roles in growth and development. Recently, we observed that fruit rinds of yellow casaba muskmelons (Cucumis melo 'Inodorous Group') accumulate naringenin chalcone, a yellow flavonoid pigment. With RNA-sequencing analysis of bulked segregants representing the tails of a population segregating for naringenin chalcone accumulation followed by fine mapping and genetic transformation, we identified a Kelch domain-containing F-box protein coding (CmKFB) gene that, when expressed, negatively regulates naringenin chalcone accumulation. Additional metabolite analysis indicated that downstream flavonoids are accumulated together with naringenin chalcone, whereas CmKFB expression diverts the biochemical flux toward coumarins and general phenylpropanoids. These results show that CmKFB functions as a posttranscriptional regulator that diverts flavonoid metabolic flux.

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Lessons from Fungal F-Box Proteins

Cited by 81 publications

References 218 publications

A new regulatory pathway of mRNA export by an F-box protein, Mdm30

A new regulatory pathway of mRNA export by an F-box protein, Mdm30

The Casein Kinase I Protein Cck1 Regulates Multiple Signaling Pathways and Is Essential for Cell Integrity and Fungal Virulence in Cryptococcus neoformans

A Kelch domain-containing F-box coding gene negatively regulates flavonoid accumulation in Cucumis melo L.

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