Stress granules

Stress granules are aggregates composed of proteins and RNA molecules – mostly stalled translation initiation complexes – that usually form in a reversible manner upon cellular stress. Stress granules can also precipitate the formation of toxic protein aggregates such as those seen during the progression of certain types of neurological disease.

Latest Research and Reviews

  • Reviews |

    Recent studies have highlighted the contribution of RNA to cellular liquid–liquid phase separation and condensate formation. RNA features modulate the composition and biophysical properties of RNA–protein condensates, which have various cellular functions, including RNA transport and localization, supporting catalytic processes and responding to stress.

    • Christine Roden
    •  & Amy S. Gladfelter
  • Research |

    Gaglia et al. show, using single-cell imaging and analysis in human tumours, that phase transition of heat-shock factor 1 (HSF1) to form intranuclear stress bodies mediates cell-fate decisions underlying cell survival or death.

    • Giorgio Gaglia
    • , Rumana Rashid
    • , Clarence Yapp
    • , Gaurav N. Joshi
    • , Carmen G. Li
    • , Susan L. Lindquist
    • , Kristopher A. Sarosiek
    • , Luke Whitesell
    • , Peter K. Sorger
    •  & Sandro Santagata
    Nature Cell Biology 22, 151-158
  • Reviews |

    RNA-binding proteins regulate the use of mRNA during periods of stress, in part through the formation of transient membraneless organelles known as stress granules. In this Review, Wolozin and Ivanov examine the biology of such granules in neurons and their potential roles in a number of neurodegenerative diseases.

    • Benjamin Wolozin
    •  & Pavel Ivanov
  • Research
    | Open Access

    Alborz Mazloomian et al. use small molecule inhibitors to disrupt EIF4A3’s ATPase and helicase function which affects alternative splicing and nonsense mediated decay of transcripts. They define a genome-wide pattern of motifs of RNA-binding proteins associated with EIF4A3 and find that stress granules are downregulated upon EIF4A3 inhibition.

    • Alborz Mazloomian
    • , Shinsuke Araki
    • , Momoko Ohori
    • , Amal M. El-Naggar
    • , Damian Yap
    • , Ali Bashashati
    • , Shoichi Nakao
    • , Poul H. Sorensen
    • , Atsushi Nakanishi
    • , Sohrab Shah
    •  & Samuel Aparicio
  • Research
    | Open Access

    Low complexity (LC) domains can drive the formation of both amyloid fibrils and protein droplets. Here, the authors identify reversible amyloid cores from the LC of hnRNPA1, based on which they elucidate the structural basis of reversible fibrillation and its interplay with hnRNPA1 droplet formation.

    • Xinrui Gui
    • , Feng Luo
    • , Yichen Li
    • , Heng Zhou
    • , Zhenheng Qin
    • , Zhenying Liu
    • , Jinge Gu
    • , Muyun Xie
    • , Kun Zhao
    • , Bin Dai
    • , Woo Shik Shin
    • , Jianhua He
    • , Lin He
    • , Lin Jiang
    • , Minglei Zhao
    • , Bo Sun
    • , Xueming Li
    • , Cong Liu
    •  & Dan Li

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