The transcriptional regulator of the chaperone response HSF1 controls hepatic bioenergetics and protein homeostasis.

ABSTRACT: Metabolic energy reprogramming facilitates adaptations to a variety of stress conditions and cellular dysfunction, but how the energetic demands are monitored and met in response to physiological stimuli remains elusive. Our data support a model demonstrating that heat shock factor 1 (HSF1), a master transcriptional regulator of the chaperone response, has been coopted from its role as a critical protein quality-control regulator to having a central role in systemic energy sensing and for metabolic adaptation to nutrient availability. We found that in the absence of HSF1, levels of NAD⁺ and ATP are not efficiently sustained in hepatic cells, largely because of transcriptional repression of nicotinamide phosphoribosyltransferase in the NAD⁺ salvage pathway. Mechanistic

SUBMITTER: Qiao A 

PROVIDER: S-EPMC5350514 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature