AI Article Synopsis

  • Stress granules (SGs) are important cellular structures that help cells survive stress by sequestering non-translating mRNAs and proteins.
  • The study identifies UBAP2L as a key protein involved in SG formation, showing that its absence disrupts SG organization.
  • UBAP2L works with G3BP1 and small nucleolar RNAs (snoRNAs) to form a protein-RNA complex necessary for SG assembly, indicating that snoRNAs are crucial for this process.

Article 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 that snoRNAs were required for UBAP2L association with G3BP1. In addition, decreased expression of snoRNAs reduced the interaction between UBAP2L and G3BP1 and suppressed SG formation. Our results reveal a critical role of SG component, the UBAP2L/snoRNA/G3BP1 protein-RNA complex, and provide new insights into the regulation of SG assembly.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10104854PMC
http://dx.doi.org/10.1038/s42003-023-04754-wDOI Listing

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