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ProteomicsEndogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology
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 UB...
ORGANISM(S): Homo sapiens (Human) 
2025-06-04 | PXD061852 | Pride
Stress granules Retrotransposon-derived proteins Ubiquilins 
UnknownCytosolic stress granules relieve the ubiquitin-proteasome system in the nuclear compartment.
Not available
S-EPMC9890234 | biostudies-literature
ProteomicsUbiquitination regulates granulostasis and DRiP accumulation in SGs under heat stress via the E3 ligase MKRN2
Stress granules (SGs) are transient cytoplasmic biomolecular condensates that play a role in the cellular response to proteotoxic stress. It has been previously shown that ubiquitination regulates SG dynamics; however, the specific mechanisms by which ubiquitin affects SGs are not fully understood. ...
ORGANISM(S): Homo sapiens (Human) 
2026-09-09 | PXD076622 | Pride
Stress granules ubiquitin 
UnknownSequestration of highly expressed mRNAs in cytoplasmic granules, P-bodies, and stress granules enhances cell viability.
Not available
S-EPMC3285586 | biostudies-literature
UnknownCoupling of translation quality control and mRNA targeting to stress granules.
Not available
S-EPMC7401812 | biostudies-literature
TranscriptomicsChromatin immunoprecipitation of human HEK293 cells with flag-tagged IMP1 antibody
Isolation of IMP1 bound mRNAs. Flag-tagged IMP1 was expressed in HEK293 cells. Flag tagged IMP1 was immunoprecipitated and mRNAs isolated. As controls HEK293 cells that do not express Flag-tagged IMP1 was included.
ORGANISM(S): Homo sapiens 
2006-12-31 | E-MEXP-841 | biostudies-arrayexpress
UnknownNew roles for the de-ubiquitylating enzyme OTUD4 in an RNA-protein network and RNA granules.
Not available
S-EPMC6602300 | biostudies-literature
UnknownEndogenous retrovirus-like proteins recruit UBQLN2 to stress granules and shape their functional biology.
Not available
S-EPMC12273755 | biostudies-literature
UnknownStress routes clients to the proteasome via a BAG2 ubiquitin-independent degradation condensate.
Not available
S-EPMC9163039 | biostudies-literature
UnknownUBAP2L contributes to formation of P-bodies and modulates their association with stress granules.
Not available
S-EPMC11248227 | biostudies-literature
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