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HSF1 critically attunes proteotoxic stress sensing by mTORC1 to combat stress and promote growth.

Nat. Cell Biol.. 2016; 
SuKuo-Hui,CaoJunyue,TangZijian,DaiSiyuan,HeYishu,SampsonStephen Byers,BenjaminIvor J,DaiChen
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Catalog Antibody 2), HA-tag (GTX115044), or Myc-tag (A00704) antibodies, and 20 µl Protein G MagBeads (GenScript) at 4 ◦ C overnight.... Total 1 mg proteins in sonication buffer supplemented with protease inhibitor cocktail were incubated with 1 µg primary antibodies and 20 µl Protein G MagBeads (GenScript) at 4 ◦ C overnight. Get A Quote

摘要

To cope with proteotoxic stress, cells attenuate protein synthesis. However, the precise mechanisms underlying this fundamental adaptation remain poorly defined. Here we report that mTORC1 acts as an immediate cellular sensor of proteotoxic stress. Surprisingly, the multifaceted stress-responsive kinase JNK constitutively associates with mTORC1 under normal growth conditions. On activation by proteotoxic stress, JNK phosphorylates both RAPTOR at S863 and mTOR at S567, causing partial disintegration of mTORC1 and subsequent translation inhibition. Importantly, HSF1, the central player in the proteotoxic stress response (PSR), preserves mTORC1 integrity and function by inactivating JNK, independ... More

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