PXD061852 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Endogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology |
Description | The human genome is replete with sequences derived from foreign elements including endogenous retrovirus-like proteins of unknown function. The human genome is replete with sequences derived from foreign elements including endogenous retrovirus-like proteins of unknown function. Here we show that UBQLN2, a ubiquitin-proteasome shuttle factor implicated in neurodegenerative diseases, is regulated by the linked actions of two retrovirus-like proteins, RTL8 and PEG10. RTL8 confers on UBQLN2 the ability to complex with and regulate PEG10. PEG10, a core component of stress granules, drives the recruitment of UBQLN2 to stress granules under various stress conditions, but can only do so when RTL8 is present. Changes in PEG10 levels further remodel the kinetics of stress granule disassembly and overall composition by incorporating select extracellular vesicle proteins. Within stress granules, PEG10 forms virus-like particles, underscoring the structural heterogeneity of this class of biomolecular condensates. Together, these results reveal an unexpected link between pathways of cellular proteostasis and endogenous retrovirus-like proteins. we show that UBQLN2, a ubiquitin-proteasome shuttle factor implicated in neurodegenerative diseases, is regulated by the linked actions of two retrovirus-like proteins, RTL8 and PEG10. RTL8 confers on UBQLN2 the ability to complex with and regulate PEG10. PEG10, a core component of stress granules, drives the recruitment of UBQLN2 to stress granules under various stress conditions, but can only do so when RTL8 is present. Changes in PEG10 levels further remodel the kinetics of stress granule disassembly and overall composition by incorporating select extracellular vesicle proteins. Within stress granules, PEG10 forms virus-like particles, underscoring the structural heterogeneity of this class of biomolecular condensates. Together, these results reveal an unexpected link between pathways of cellular proteostasis and endogenous retrovirus-like proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2025-06-04 |
AnnouncementXML | Submission_2025-06-04_08:42:56.673.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lisa Sharkey |
SpeciesList | scientific name: Homo sapiens (Human); NCBI TaxID: 9606; |
ModificationList | monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | Orbitrap Fusion; Orbitrap Ascend |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2025-03-14 10:11:58 | ID requested | |
⏵ 1 | 2025-06-04 08:42:57 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: stress granules, retrotransposon-derived proteins,Ubiquilins |
Contact List
Lisa M. Sharkey |
contact affiliation | Department of Neurology, University of Michigan Medical School, Ann Arbor, MI 48109, United States |
contact email | lisams@umich.edu |
lab head | |
Lisa Sharkey |
contact affiliation | University of Michigan |
contact email | lisams@umich.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD061852
- Label: PRIDE project
- Name: Endogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology