<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Riggs CL</submitter><funding>National Institutes of General Medical Sciences</funding><pagination>e202307146</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11248227</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>223(10)</volume><pubmed_abstract>Stress triggers the formation of two distinct cytoplasmic biomolecular condensates: stress granules (SGs) and processing bodies (PBs), both of which may contribute to stress-responsive translation regulation. Though PBs can be present constitutively, stress can increase their number and size and lead to their interaction with stress-induced SGs. The mechanism of such interaction, however, is largely unknown. Formation of canonical SGs requires the RNA binding protein Ubiquitin-Associated Protein 2-Like (UBAP2L), which is a central SG node protein in the RNA-protein interaction network of SGs and PBs. UBAP2L binds to the essential SG and PB proteins G3BP and DDX6, respectively. Research on UBAP2L has mostly focused on its role in SGs, but not its connection to PBs. We find that UBAP2L is no</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>UBAP2L contributes to formation of P-bodies and modulates their association with stress granules.</pubmed_title><pmcid>PMC11248227</pmcid><funding_grant_id>R01 GM126150</funding_grant_id><funding_grant_id>F32GM142262</funding_grant_id><funding_grant_id>K99GM148723</funding_grant_id><funding_grant_id>R01 GM146997</funding_grant_id><funding_grant_id>R35GM12901</funding_grant_id><pubmed_authors>Zubair SN</pubmed_authors><pubmed_authors>Anderson P</pubmed_authors><pubmed_authors>Amarsanaa M</pubmed_authors><pubmed_authors>Ivanov P</pubmed_authors><pubmed_authors>Riggs CL</pubmed_authors><pubmed_authors>Kedersha N</pubmed_authors></additional><is_claimable>false</is_claimable><name>UBAP2L contributes to formation of P-bodies and modulates their association with stress granules.</name><description>Stress triggers the formation of two distinct cytoplasmic biomolecular condensates: stress granules (SGs) and processing bodies (PBs), both of which may contribute to stress-responsive translation regulation. Though PBs can be present constitutively, stress can increase their number and size and lead to their interaction with stress-induced SGs. The mechanism of such interaction, however, is largely unknown. Formation of canonical SGs requires the RNA binding protein Ubiquitin-Associated Protein 2-Like (UBAP2L), which is a central SG node protein in the RNA-protein interaction network of SGs and PBs. UBAP2L binds to the essential SG and PB proteins G3BP and DDX6, respectively. Research on UBAP2L has mostly focused on its role in SGs, but not its connection to PBs. We find that UBAP2L is no</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Oct</publication><modification>2025-04-25T19:20:12.818Z</modification><creation>2025-04-06T07:54:45.355Z</creation></dates><accession>S-EPMC11248227</accession><cross_references><pubmed>39007803</pubmed><doi>10.1083/jcb.202307146</doi></cross_references></HashMap>