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HDAC6-ubiquitin interaction controls the duration of HSF1 activation after heat shock.

Pernet L, Faure V, Gilquin B, Dufour-Guérin S, Khochbin S, Vourc'h C - Mol. Biol. Cell (2014)

Bottom Line: Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is itself controlled by HDAC6, a unique deacetylase known to bind monoubiquitin and polyubiquitin with high affinity.In cells expressing HDAC6 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of HSF1, precluding late activation of the HSP25 gene.In these cells, knockdown of p97/VCP rescues HSF1 from this rapid inactivation and restores HSP25 expression.

View Article: PubMed Central - PubMed

Affiliation: University Grenoble-Alpes, CRI INSERM, U823, Institut Albert Bonniot, La Tronche 38042, Grenoble Cedex 9, France.

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p97/VCP is required to knock down HSP25 accumulation in Ubm heat-shocked cell line. WT and Ubm cells were submitted or not (NHS) to heat shock, followed by different conditions of recovery (Rec) at 37°C. Ubm HDAC6–expressing cells were transfected with a siRNA against p97/VCP. HSP25 expression was analyzed by Western blot with an anti-HSP25 antibody. The efficiency of the sip97/VCP knockdown was assessed by Western blot using an anti-p97/VCP antibody. Tubulin was used as loading control.
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Figure 4: p97/VCP is required to knock down HSP25 accumulation in Ubm heat-shocked cell line. WT and Ubm cells were submitted or not (NHS) to heat shock, followed by different conditions of recovery (Rec) at 37°C. Ubm HDAC6–expressing cells were transfected with a siRNA against p97/VCP. HSP25 expression was analyzed by Western blot with an anti-HSP25 antibody. The efficiency of the sip97/VCP knockdown was assessed by Western blot using an anti-p97/VCP antibody. Tubulin was used as loading control.

Mentions: In contrast, we observed complete rescue of HSP25 expression in heat-shocked HDAC6 Ubm–expressing cells treated with sip97/VCP (Figure 4).


HDAC6-ubiquitin interaction controls the duration of HSF1 activation after heat shock.

Pernet L, Faure V, Gilquin B, Dufour-Guérin S, Khochbin S, Vourc'h C - Mol. Biol. Cell (2014)

p97/VCP is required to knock down HSP25 accumulation in Ubm heat-shocked cell line. WT and Ubm cells were submitted or not (NHS) to heat shock, followed by different conditions of recovery (Rec) at 37°C. Ubm HDAC6–expressing cells were transfected with a siRNA against p97/VCP. HSP25 expression was analyzed by Western blot with an anti-HSP25 antibody. The efficiency of the sip97/VCP knockdown was assessed by Western blot using an anti-p97/VCP antibody. Tubulin was used as loading control.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

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getmorefigures.php?uid=PMC4263459&req=5

Figure 4: p97/VCP is required to knock down HSP25 accumulation in Ubm heat-shocked cell line. WT and Ubm cells were submitted or not (NHS) to heat shock, followed by different conditions of recovery (Rec) at 37°C. Ubm HDAC6–expressing cells were transfected with a siRNA against p97/VCP. HSP25 expression was analyzed by Western blot with an anti-HSP25 antibody. The efficiency of the sip97/VCP knockdown was assessed by Western blot using an anti-p97/VCP antibody. Tubulin was used as loading control.
Mentions: In contrast, we observed complete rescue of HSP25 expression in heat-shocked HDAC6 Ubm–expressing cells treated with sip97/VCP (Figure 4).

Bottom Line: Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is itself controlled by HDAC6, a unique deacetylase known to bind monoubiquitin and polyubiquitin with high affinity.In cells expressing HDAC6 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of HSF1, precluding late activation of the HSP25 gene.In these cells, knockdown of p97/VCP rescues HSF1 from this rapid inactivation and restores HSP25 expression.

View Article: PubMed Central - PubMed

Affiliation: University Grenoble-Alpes, CRI INSERM, U823, Institut Albert Bonniot, La Tronche 38042, Grenoble Cedex 9, France.

Show MeSH
Related in: MedlinePlus