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Cyril Boyault

Researcher at French Institute of Health and Medical Research

Publications -  8
Citations -  1237

Cyril Boyault is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Ubiquitin & Acetylation. The author has an hindex of 6, co-authored 8 publications receiving 1123 citations. Previous affiliations of Cyril Boyault include Joseph Fourier University.

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HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates.

TL;DR: The data show that HDAC6 senses ubiquitinated cellular aggregates and consequently induces the expression of major cellular chaperones by triggering the dissociation of a repressive HDAC 6/HSF1/HSP90 (heat-shock protein 90) complex and a subsequent HSF1 activation, andHDAC6 appears as a master regulator of the cell protective response to cytotoxic protein aggregate formation.
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HDAC6–p97/VCP controlled polyubiquitin chain turnover

TL;DR: It is proposed that a finely tuned balance of HDAC6 and p97/VCP concentrations determines the fate of ubiquitinated misfolded proteins: p97 /VCP would promote protein degradation and ubiquitin turnover, whereasHDAC6 would favour the accumulation of ubiquITinated protein aggregates and inclusion body formation.
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Regulatory cross-talk between lysine acetylation and ubiquitination: role in the control of protein stability.

TL;DR: Analysis of the underlying mechanisms shows that, besides a direct competition between the two lysine modifications, more complex and indirect processes also connect these two signalling pathways.
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Regulation of protein turnover by acetyltransferases and deacetylases

TL;DR: Observations reveal a tight link between protein lysine acetylation and ubiquitination and designate theacetylation machinery as a determinant element in the control of cellular proteolytic activities.
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Heat-Shock Factor 1 Controls Genome-wide Acetylation in Heat-shocked Cells

TL;DR: HSF1 is identified as a master regulator of global chromatin acetylation and a cross-talk between HSF1 and histone deacetylases in the general control of genome organization in response to heat shock is revealed.