{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Asano-Inami E"],"funding":["MEXT | Japan Society for the Promotion of Science"],"pagination":["415"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10104854"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(1)"],"pubmed_abstract":["Stress granules (SGs) are dynamic, non-membranous structures composed of non-translating mRNAs and various proteins and play critical roles in cell survival under stressed conditions. Extensive proteomics analyses have been performed to identify proteins in SGs; however, the molecular functions of these components in SG formation remain unclear. In this report, we show that ubiquitin-associated protein 2-like (UBAP2L) is a crucial component of SGs. UBAP2L localized to SGs in response to various stresses, and its depletion significantly suppressed SG organization. Proteomics and RNA sequencing analyses found that UBAP2L formed a protein-RNA complex with Ras-GTP-activating protein SH3 domain binding protein 1 (G3BP1) and small nucleolar RNAs (snoRNAs). In vitro binding analysis demonstrated "],"journal":["Communications biology"],"pubmed_title":["The association of UBAP2L and G3BP1 mediated by small nucleolar RNA is essential for stress granule formation."],"pmcid":["PMC10104854"],"funding_grant_id":["21H03075"],"pubmed_authors":["Hamaguchi T","Kajiyama H","Hyodo T","Yokoi A","Asano-Inami E","Sugiyama M"],"additional_accession":[]},"is_claimable":false,"name":"The association of UBAP2L and G3BP1 mediated by small nucleolar RNA is essential for stress granule formation.","description":"Stress granules (SGs) are dynamic, non-membranous structures composed of non-translating mRNAs and various proteins and play critical roles in cell survival under stressed conditions. Extensive proteomics analyses have been performed to identify proteins in SGs; however, the molecular functions of these components in SG formation remain unclear. In this report, we show that ubiquitin-associated protein 2-like (UBAP2L) is a crucial component of SGs. UBAP2L localized to SGs in response to various stresses, and its depletion significantly suppressed SG organization. Proteomics and RNA sequencing analyses found that UBAP2L formed a protein-RNA complex with Ras-GTP-activating protein SH3 domain binding protein 1 (G3BP1) and small nucleolar RNAs (snoRNAs). In vitro binding analysis demonstrated ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Apr","modification":"2025-04-04T23:00:27.218Z","creation":"2025-04-04T23:00:27.218Z"},"accession":"S-EPMC10104854","cross_references":{"pubmed":["37059803"],"doi":["10.1038/s42003-023-04754-w"]}}