A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.

@article{Ganassi2016ASF,
  title={A Surveillance Function of the HSPB8-BAG3-HSP70 Chaperone Complex Ensures Stress Granule Integrity and Dynamism.},
  author={Massimo Ganassi and Daniel Matějů and Ilaria Bigi and Laura Mediani and Ina Poser and Hyun Ok Lee and Samuel J. Seguin and Federica Francesca Morelli and Jonathan Vinet and Giuseppina Leo and Orietta Pansarasa and Alberto Petrucci and Angelo Poletti and Stephano Alberti and Serena Carra},
  journal={Molecular cell},
  year={2016},
  volume={63 5},
  pages={
          796-810
        }
}
Stress granules (SGs) are ribonucleoprotein complexes induced by stress. They sequester mRNAs and disassemble when the stress subsides, allowing translation restoration. In amyotrophic lateral sclerosis (ALS), aberrant SGs cannot disassemble and therefore accumulate and are degraded by autophagy. However, the molecular events causing aberrant SG formation and the molecular players regulating this transition are largely unknown. We report that defective ribosomal products (DRiPs) accumulate in… CONTINUE READING
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