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TitleISRIB Blunts the Integrated Stress Response by Allosterically Antagonising the Inhibitory Effect of Phosphorylated eIF2 on eIF2B.
Journal, issue, pagesMol Cell, Vol. 81, Issue 1, Page 88-103.e6, Year 2021
Publish dateJan 7, 2021
AuthorsAlisa F Zyryanova / Kazuhiro Kashiwagi / Claudia Rato / Heather P Harding / Ana Crespillo-Casado / Luke A Perera / Ayako Sakamoto / Madoka Nishimoto / Mayumi Yonemochi / Mikako Shirouzu / Takuhiro Ito / David Ron /
PubMed AbstractThe small molecule ISRIB antagonizes the activation of the integrated stress response (ISR) by phosphorylated translation initiation factor 2, eIF2(αP). ISRIB and eIF2(αP) bind distinct sites in ...The small molecule ISRIB antagonizes the activation of the integrated stress response (ISR) by phosphorylated translation initiation factor 2, eIF2(αP). ISRIB and eIF2(αP) bind distinct sites in their common target, eIF2B, a guanine nucleotide exchange factor for eIF2. We have found that ISRIB-mediated acceleration of eIF2B's nucleotide exchange activity in vitro is observed preferentially in the presence of eIF2(αP) and is attenuated by mutations that desensitize eIF2B to the inhibitory effect of eIF2(αP). ISRIB's efficacy as an ISR inhibitor in cells also depends on presence of eIF2(αP). Cryoelectron microscopy (cryo-EM) showed that engagement of both eIF2B regulatory sites by two eIF2(αP) molecules remodels both the ISRIB-binding pocket and the pockets that would engage eIF2α during active nucleotide exchange, thereby discouraging both binding events. In vitro, eIF2(αP) and ISRIB reciprocally opposed each other's binding to eIF2B. These findings point to antagonistic allostery in ISRIB action on eIF2B, culminating in inhibition of the ISR.
External linksMol Cell / PubMed:33220178 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.3 Å
Structure data

30568

7d43

EMDB-30568, PDB-7d43:
eIF2B-eIF2(aP), aPg complex
Method: EM (single particle) / Resolution: 4.3 Å

30569

7d44

EMDB-30569, PDB-7d44:
eIF2B-eIF2(aP), aP2 complex
Method: EM (single particle) / Resolution: 4.0 Å

30570

7d45

EMDB-30570, PDB-7d45:
eIF2B-eIF2(aP), aP1 complex
Method: EM (single particle) / Resolution: 3.8 Å

30571

7d46

EMDB-30571, PDB-7d46:
eIF2B apo
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsTRANSLATION / Complex / Translational control

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