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DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation

ABSTRACT: DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation

PROVIDER: PRJNA1211158 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR32015926_1.fastq.gz	Fastqsanger.gz
	SRR32015926_2.fastq.gz	Fastqsanger.gz
	SRR32015927_1.fastq.gz	Fastqsanger.gz
	SRR32015927_2.fastq.gz	Fastqsanger.gz
	SRR32015928_1.fastq.gz	Fastqsanger.gz

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DNA binding and mitotic phosphorylation protect polyglutamine proteins from assembly formation

Project description:Polyglutamine expansion is associated with pathogenic protein aggregation in neurodegenerative disorders. However, long polyglutamine tracts are also found in many transcription factors (TFs), such as FOXP2, a TF implicated in human speech. Here, we explore how FOXP2 and other glutamine-rich TFs avoid unscheduled assembly. Throughout interphase, DNA binding, irrespective of sequence specificity, has a solubilizing effect. During mitosis, multiple phosphorylation events promote FOXP2’s eviction from chromatin and supplant the solubilizing function of DNA. Further, human-specific amino-acid substitutions linked to the evolution of speech map to a mitotic phospho-patch, the ‘EVO patch’, and reduce the propensity of the human FOXP2 to assemble. Fusing the pathogenic form of Huntingtin to either a DNA binding domain, a phospho-mimetic variant of this ‘EVO patch’ or a negatively charged peptide is sufficient to diminish assembly formation, suggesting that hijacking mechanisms governing solubility of glutamine-rich TFs may offer new strategies for treatment of polyQ expansion diseases.

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Dynamic phosphorylation of FOXA1 by Aurora B guides post-mitotic gene reactivation

Project description:FOXA1 serves as a crucial pioneer transcription factor in developmental processes, and plays a pivotal role as a mitotic bookmarking factor to perpetuate gene expression profiles and maintain cellular identity. During mitosis, the majority of FOXA1 dissociates from specific DNA binding sites and redistributes to non-specific binding sites, however, the regulatory mechanisms governing FOXA1's molecular dynamics in mitosis remain elusive. Here we show that mitotic kinase Aurora B regulates FOXA1's different DNA binding modes and the formation of the biomolecular condensate. Mechanistically, Aurora B kinase phosphorylates FOXA1 at Serine 221 (S221) to disrupt the specific, but not the non-specific, DNA binding. The phosphorylation of S221 also negatively regulates the FOXA1 condensates that require specific DNA binding. Importantly, perturbation of the dynamic phosphorylation impairs accurate gene reactivations and cell proliferation, suggesting that reversible mitotic protein phosphorylation emerges as a fundamental mechanism for the spatiotemporal control of mitotic bookmarking.

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