Proteomics

Dataset Information

0

Membrane atg8ylation coordinates stress granule formation and mTOR inactivation in response to lysosomal damage

ABSTRACT: We report that lysosomal damage is a hitherto unknown inducer of stress granule (SG) formation and that the process termed membrane atg8ylation coordinates SG formation with mTOR inactivation during lysosomal stress. SGs were induced by lysosome-damaging agents including SARS-CoV-2ORF3a, Mycobacterium tuberculosis, and proteopathic tau. During damage, mammalian ATG8s directly interacted with the core SG proteins NUFIP2 and G3BP1. Atg8ylation was needed for their recruitment to damaged lysosomes independently of SG condensates whereupon NUFIP2 contributed to mTOR inactivation via the Ragulator-RagA/B complex. Thus, cells employ membrane atg8ylation to control and coordinate SG and mTOR responses to lysosomal damage.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Vojo Deretic  

PROVIDER: MSV000089622 | MassIVE | Thu Jun 09 12:36:00 BST 2022

SECONDARY ACCESSION(S): PXD034414

REPOSITORIES: MassIVE

Json Xml

Dataset's files

Source:
Action DRS
Other
Items per page:
1 - 1 of 1
altmetric image

Publications

Stress granules and mTOR are regulated by membrane atg8ylation during lysosomal damage.

Jia Jingyue J   Wang Fulong F   Bhujabal Zambarlal Z   Peters Ryan R   Mudd Michal M   Duque Thabata T   Allers Lee L   Javed Ruheena R   Salemi Michelle M   Behrends Christian C   Phinney Brett B   Johansen Terje T   Deretic Vojo V  

The Journal of cell biology 20220930 11

We report that lysosomal damage is a hitherto unknown inducer of stress granule (SG) formation and that the process termed membrane atg8ylation coordinates SG formation with mTOR inactivation during lysosomal stress. SGs were induced by lysosome-damaging agents including SARS-CoV-2ORF3a, Mycobacterium tuberculosis, and proteopathic tau. During damage, mammalian ATG8s directly interacted with the core SG proteins NUFIP2 and G3BP1. Atg8ylation was needed for their recruitment to damaged lysosomes  ...[more]

Similar Datasets

Proteomics Atg8ylation coordinates stress granule formation and mTOR inactivation in response to lysosomal damage
| MSV000088152 | MassIVE
Proteomics A mechanism that transduces lysosomal damage signals to stress granule formation for cell survival
2024-01-04 | MSV000093768 | MassIVE
Transcriptomics Gadd45β is critical for regulation of type I interferon signaling by facilitating G3BP-mediated stress granule formation
2024-09-06 | GSE242462 | GEO
Proteomics Galectins control mTOR in response to endomembrane damage
2017-12-07 | MSV000081788 | MassIVE
Transcriptomics G3BP1 translocates into mitochondria to impair MCU complex function and promotes NASH progression
2023-12-13 | GSE249869 | GEO
Transcriptomics G3BP1 translocates into mitochondria to impair MCU complex function and promotes NASH progression [G3bp1-HKO and G3bp1-Flox mice with BSA or PA treatment]
2024-08-18 | GSE274650 | GEO
Transcriptomics Diverse CMT2 Neuropathies are Linked to Aberrant G3BP Interactions in Stress Granules
2023-02-03 | GSE220821 | GEO
Transcriptomics ECT2 and AURKB Modulate Formation of Stress Granules Containing Transcripts from Diverse Cellular Pathways in Astrocytoma Cells
2016-02-29 | E-GEOD-76814 | biostudies-arrayexpress
Proteomics Triple SILAC based quantitative MS approach to determine Withaferin A regulated proteins in prostate cancer
2021-07-21 | PXD016759 | Pride
Proteomics No evidence for the presence and control of tumor growth by stress granules in Kras mutant cancers
2024-09-24 | PXD053882 | Pride