Prepare an open-source resource for interrogation of the druggable human GPCR-ome
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Baird et al. – 2014 – HSF-1-mediated cytoskeletal integrity determines thermotolerance and life span
Discovered that thermotolerance is regulated by HSF-1 but not through upregulation of heat shock proteins as previously thought.
They authors used molecular biology techniques such as PCR, plasmid construction methods, etc. to show that truncated versions of the HSF-1 gene have decreased transcriptional activity in C. elegans.
Fig 1. Only the full-length HSF-1 gene leads to heat shock protein expression, however both full length and truncated genes increase thermotolerance and life span.
Fig 2. HSF-1 regulates PAT-10 expression. Knock out of PAT-10 causes a decrease in thermotolerance and overexpression increases thermotolerance. The PAT-10 effect is independent of heat shock proteins.
Fig 3. Use fluorescence microscopy and GFP to assess the actin cytoskeleton. Loss of PAT-10 leads to a messed-up actin cytoskeleton when animals were heat stressed.
Overexpression of PAT-10 protected the actin cytoskeleton from heat stress. Overexpression also delayed the decrease in F actin that is normally seen with aging.
Fig 4. Using pharmacology they showed that disrupting the actin cytoskeleton in human cells also impaired their thermotolerance.
The transcription factor HSF-1 affects thermotolerance by controlling the expression of PAT-10, which is required to keep the actin cytoskeleton from collapsing. HSF-1 regulation of PAT-10 is independent of its heat shock protein responsibilities. Over-expressing PAT-10 increased thermotolerance and life span. Pathways that activate PAT-10 should be explored further because the pathway would make a good target for the treatment of age-related diseases.
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