Modulation of Heat Shock Factor 1 Activity through Silencing of Ser303/Ser307 Phosphorylation Supports a Metabolic Program Leading to Age-Related Obesity and Insulin Resistance | Zendy

Xiongjie Jin | Zendy; Aijun Qiao | Zendy; Demetrius Moskophidis | Zendy; Nahid F. Mivechi | Zendy

Open Access

Modulation of Heat Shock Factor 1 Activity through Silencing of Ser303/Ser307 Phosphorylation Supports a Metabolic Program Leading to Age-Related Obesity and Insulin Resistance

Author(s) -

Xiongjie Jin,

Aijun Qiao,

Demetrius Moskophidis,

Nahid F. Mivechi

Publication year - 2018

Publication title -

molecular and cellular biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.14

H-Index - 327

eISSN - 1067-8824

pISSN - 0270-7306

DOI - 10.1128/mcb.00095-18

Subject(s) - hsf1 , biology , proteostasis , microbiology and biotechnology , phosphorylation , heat shock , heat shock factor , gene silencing , heat shock protein , hsp70 , biochemistry , gene

Activation of the adaptive response to cellular stress orchestrated by heat shock factor 1 (HSF1), which is an evolutionarily conserved transcriptional regulator of chaperone response and cellular bioenergetics in diverse model systems, is a central feature of organismal defense from environmental and cellular stress. HSF1 activity, induced by proteostatic, metabolic, and growth factor signals, is regulated by posttranscriptional modifications, yet the mechanisms that regulate HSF1 and particularly the functional significance of these modifications in modulating its biological activityin vivo remain unknown.

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