PMID- 32989041
OWN - NLM
STAT- MEDLINE
DCOM- 20210621
LR  - 20230829
IS  - 1477-9137 (Electronic)
IS  - 0021-9533 (Print)
IS  - 0021-9533 (Linking)
VI  - 133
IP  - 20
DP  - 2020 Oct 28
TI  - UV damage induces G3BP1-dependent stress granule formation that is not driven by 
      mTOR inhibition-mediated translation arrest.
LID - 10.1242/jcs.248310 [doi]
LID - jcs248310
AB  - Translation arrest is a part of the cellular stress response that decreases 
      energy consumption and enables rapid reprioritisation of gene expression. Often 
      translation arrest leads to condensation of untranslated messenger 
      ribonucleoproteins (mRNPs) into stress granules (SGs). Studies into mechanisms of 
      SG formation and functions are complicated because various types of stress cause 
      formation of SGs with different properties and composition. In this work, we 
      focused on the mechanism of SG formation triggered by UV damage. We demonstrate 
      that UV-induced inhibition of translation does not involve inhibition of the 
      mechanistic target of rapamycin (mTOR) signaling or dissociation of the 48S 
      preinitiation complexes. The general control non-derepressible 2 (GCN2; also 
      known as EIF2AK4) kinase contributes to UV-induced SG formation, which is 
      independent of the phosphorylation of the eukaryotic translation initiation 
      factor 2alpha. Like many other types of SGs, condensation of UV-induced granules 
      requires the Ras-GTPase-activating protein SH3-domain-binding protein 1 (G3BP1). 
      Our work reveals that, in UV-treated cells, the mechanisms of translation arrest 
      and SG formation may be unlinked, resulting in SGs that do not contain the major 
      type of polysome-free preinitiation complexes that accumulate in the 
      cytoplasm.This article has an associated First Person interview with the first 
      author of the paper.
CI  - (c) 2020. Published by The Company of Biologists Ltd.
FAU - Ying, Shan
AU  - Ying S
AD  - Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H 
      4R2, Canada.
FAU - Khaperskyy, Denys A
AU  - Khaperskyy DA
AUID- ORCID: 0000-0003-0583-7179
AD  - Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H 
      4R2, Canada d.khaperskyy@dal.ca.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20201028
PL  - England
TA  - J Cell Sci
JT  - Journal of cell science
JID - 0052457
RN  - 0 (Carrier Proteins)
RN  - 0 (Poly-ADP-Ribose Binding Proteins)
RN  - 0 (RNA Recognition Motif Proteins)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - EC 3.6.4.- (DNA Helicases)
RN  - EC 3.6.4.13 (RNA Helicases)
SB  - IM
MH  - Carrier Proteins
MH  - Cytoplasmic Granules
MH  - *DNA Helicases
MH  - Poly-ADP-Ribose Binding Proteins
MH  - *RNA Helicases/genetics
MH  - RNA Recognition Motif Proteins
MH  - TOR Serine-Threonine Kinases/genetics
PMC - PMC7648617
OTO - NOTNLM
OT  - G3BP1
OT  - GCN2
OT  - Stress granule
OT  - UVC
OT  - mTOR
COIS- Competing interestsThe authors declare no competing or financial interests.
EDAT- 2020/09/30 06:00
MHDA- 2021/06/22 06:00
PMCR- 2020/10/28
CRDT- 2020/09/29 05:31
PHST- 2020/04/29 00:00 [received]
PHST- 2020/09/17 00:00 [accepted]
PHST- 2020/09/30 06:00 [pubmed]
PHST- 2021/06/22 06:00 [medline]
PHST- 2020/09/29 05:31 [entrez]
PHST- 2020/10/28 00:00 [pmc-release]
AID - jcs.248310 [pii]
AID - JCS248310 [pii]
AID - 10.1242/jcs.248310 [doi]
PST - epublish
SO  - J Cell Sci. 2020 Oct 28;133(20):jcs248310. doi: 10.1242/jcs.248310.