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dFoxo Dependent Transcription of the Heat Shock Proteins
Author(s) -
Donovan Marissa,
Marr Michael
Publication year - 2015
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.29.1_supplement.880.31
Subject(s) - proteotoxicity , hsp70 , drosophila melanogaster , heat shock protein , microbiology and biotechnology , transcription factor , heat shock , oxidative stress , biology , heat shock factor , transcription (linguistics) , gene , protein aggregation , genetics , biochemistry , linguistics , philosophy
Drosophila melanogaster accumulate large and small heat shock protein transcripts in response to oxidative damage. The large Hsp70 and the small Hsps are two different classes of molecular chaperones that protect against proteotoxicity by preventing the accumulation of mis‐folded, non‐native proteins using two separate mechanisms. Here we establish the small Hsps and Hsp70 are targets of Foxo in Drosophila. The Foxo family of pioneer transcription factors promotes cellular stress resistance in response to many conditions including oxidative stress. In response to acute oxidative stress caused by paraquat, Foxo and HSF collaborate by increasing expression of these chaperones. These data indicate a mechanism where overlapping pathways transcriptionally upregulate protective genes to promote survival.