<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Asano-Inami E</submitter><funding>MEXT | Japan Society for the Promotion of Science</funding><pagination>415</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC10104854</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>6(1)</volume><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 </pubmed_abstract><journal>Communications biology</journal><pubmed_title>The association of UBAP2L and G3BP1 mediated by small nucleolar RNA is essential for stress granule formation.</pubmed_title><pmcid>PMC10104854</pmcid><funding_grant_id>21H03075</funding_grant_id><pubmed_authors>Hamaguchi T</pubmed_authors><pubmed_authors>Kajiyama H</pubmed_authors><pubmed_authors>Hyodo T</pubmed_authors><pubmed_authors>Yokoi A</pubmed_authors><pubmed_authors>Asano-Inami E</pubmed_authors><pubmed_authors>Sugiyama M</pubmed_authors></additional><is_claimable>false</is_claimable><name>The association of UBAP2L and G3BP1 mediated by small nucleolar RNA is essential for stress granule formation.</name><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 </description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 Apr</publication><modification>2025-04-04T23:00:27.218Z</modification><creation>2025-04-04T23:00:27.218Z</creation></dates><accession>S-EPMC10104854</accession><cross_references><pubmed>37059803</pubmed><doi>10.1038/s42003-023-04754-w</doi></cross_references></HashMap>