Proteomics

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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

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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]

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