Kizuna is a novel mitotic substrate for CDC25B phosphatase

Thomas, Y.; Peter, Matthias; Méchali, Francisca; Blanchard, Jean‐Marie; Coux, Olivier; Baldin, Véronique

doi:10.4161/15384101.2014.972882

Cited by 7 publications

(8 citation statements)

References 51 publications

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“…A follow-up to this work could be identifying the CDK independent players downstream of CDC25B. Other CDC25B substrates have been characterised, such as steroid receptors ( Ma et al, 2001 ), and the peri-centriolar material component Kizuna ( Thomas et al, 2014 ). A recent analysis using microarrayed Tyr(P) peptides representing confirmed and theoretical phosphorylation motifs from the cellular proteome, identifies more than 130 potential CDC25B substrates ( Zhao et al, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Neurogenic decisions require a cell cycle independent function of the CDC25B phosphatase

Bonnet

Molina

Roussat

et al. 2018

eLife

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A fundamental issue in developmental biology and in organ homeostasis is understanding the molecular mechanisms governing the balance between stem cell maintenance and differentiation into a specific lineage. Accumulating data suggest that cell cycle dynamics play a major role in the regulation of this balance. Here we show that the G2/M cell cycle regulator CDC25B phosphatase is required in mammals to finely tune neuronal production in the neural tube. We show that in chick neural progenitors, CDC25B activity favors fast nuclei departure from the apical surface in early G1, stimulates neurogenic divisions and promotes neuronal differentiation. We design a mathematical model showing that within a limited period of time, cell cycle length modifications cannot account for changes in the ratio of the mode of division. Using a CDC25B point mutation that cannot interact with CDK, we show that part of CDC25B activity is independent of its action on the cell cycle.

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Section: Discussionmentioning

confidence: 99%

Neurogenic decisions require a cell cycle independent function of the CDC25B phosphatase

Bonnet

Molina

Roussat

et al. 2018

eLife

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“…A follow-up to this work could be to characterise the players downstream of CDC25B that are CDK independent. Other CDC25B substrates have been characterised, such as steroid receptors (Ma, Liu, Ngan, & Tsai, 2001), or the peri-centriolar material component Kizuna (Thomas et al, 2014). A recent analysis using microarrayed Tyr(P) peptides representing confirmed and theoretical phosphorylation motifs from the cellular proteome, identifies more than 130 potential CDC25B substrates (Zhao et al, 2015).…”

Section: Discussionmentioning

confidence: 99%

Neurogenic decisions require a cell cycle independent function of the CD25B phosphatase

Bonnet

Roussat

Molina

et al. 2017

Preprint

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A fundamental issue in developmental biology and in organ homeostasis is understanding the molecular mechanisms governing the balance between stem cell maintenance and differentiation into a specific lineage. Accumulating data suggest that cell cycle dynamics plays a major role in the regulation of this balance. Here we show that the G2/M cell cycle regulator CDC25B phosphatase is required in mammals to finely tune neuronal production in the neural tube. We show that in chick neural progenitors, CDC25B activity is both required and sufficient to stimulate neurogenic divisions and to promote neuronal differentiation. We design a mathematical model showing that within a limited period of time, cell cycle length modifications cannot account for changes in the ratio of the mode of division. Using a CDC25B point mutation that cannot interact with CDK, we show that part of CDC25B activity on neurogenic divisions is independent of its action on the cell cycle.

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“…Single clones were then expanded and analyzed by western blotting using PA28γ antibodies. Synchronization of cells at the G1/S phase transition was performed by double thymidine block as described (Thomas et al, 2014). For Fluorescence-Activated Cell Sorting (FACS) analysis, cells were fixed with 70% ethanol and conserved at −20°C.…”

Section: Methodsmentioning

confidence: 99%

The 20S proteasome activator PA28γ controls the compaction of chromatin

Fesquet

Llères

Grimaud

et al. 2019

Preprint

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The nuclear PA28γ is known to activate the 20S proteasome, but its precise cellular functions remains unclear. Here, we identify PA28γ as a key factor that structures heterochromatin. We find that in human cells, a fraction of PA28γ-20S proteasome complexes localizes within HP1-linked heterochromatin foci. Our biochemical studies show that PA28γ interacts with HP1 proteins, particularly HP1β, which recruits the PA28γ-20S proteasome complexes to heterochromatin. Loss of PA28γ does not modify the localization of HP1β, its mobility within nuclear foci, or the level of H3K9 tri-methylation, but reduces H4K20 mono-and trimethylation, modifications involved in heterochromatin establishment. Concordantly, using a quantitative FRET-based microscopy assay to monitor nanometer-scale proximity between nucleosomes in living cells, we find that PA28γ regulates nucleosome proximity within heterochromatin, and thereby controls its compaction. This function of PA28γ is independent of the 20S proteasome. Importantly, HP1β on its own is unable to drive heterochromatin compaction without PA28γ. Combined, our data reveal an unexpected chromatin structural role of PA28γ, and provide new insights into the mechanism that controls HP1β-mediated heterochromatin compaction.

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Kizuna is a novel mitotic substrate for CDC25B phosphatase

Cited by 7 publications

References 51 publications

Neurogenic decisions require a cell cycle independent function of the CDC25B phosphatase

Neurogenic decisions require a cell cycle independent function of the CDC25B phosphatase

Neurogenic decisions require a cell cycle independent function of the CD25B phosphatase

The 20S proteasome activator PA28γ controls the compaction of chromatin

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