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. Author manuscript; available in PMC: 2013 Apr 3.
Published in final edited form as: Cell. 2012 Jan 20;148(1-2):322–334. doi: 10.1016/j.cell.2011.12.019

Figure 6. Model of HSF-1 activation regulated by IIS in C. elegans.

Figure 6

Upon heat stress stimulation, HSF-1 undergoes oligomerization, post-translational modification, and nuclear translocation in an undefined order before acquiring DNA-binding and transcriptional activity. The formation of a DDL-1 containing HSF-1 inhibitory complex (DHIC), consisting of HSF-1, HSB-1, DDL-1 and DDL-2, reduces the pool of HSF-1 susceptible to heat stress stimulation. Increased insulin/IGF-1-like signaling (IIS) promotes the formation of DHIC, while reducing DAF-2 activity promotes DDL-1 phosphorylation and disrupts DHIC formation and consequently increases HSF-1 activity under both stressed and unstressed conditions.