Scientific article

UBAP2L forms distinct cores that act in nucleating stress granules upstream of G3BP1

Published inCurrent Biology, vol. 30, no. 4, p. 698-707.e6
Publication date2020

Stress granules (SGs) are membraneless organelles that form in eukaryotic cells after stress exposure [1] (reviewed in [2-4]). Following translation inhibition, polysome disassembly releases 48S preinitiation complexes (PICs). mRNA, PICs, and other proteins coalesce in SG cores [1, 5-7]. SG cores recruit a dynamic shell, whose properties are dominated by weak interactions between proteins and RNAs [8-10]. The structure and assembly of SGs and how different components contribute to their formation are not fully understood. Using super-resolution and expansion microscopy, we find that the SG component UBAP2L [11, 12] and the core protein G3BP1 [5, 11-13] occupy different domains inside SGs. UBAP2L displays typical properties of a core protein, indicating that cores of different compositions coexist inside the same granule. Consistent with a role as a core protein, UBAP2L is required for SG assembly in several stress conditions. Our reverse genetic and cell biology experiments suggest that UBAP2L forms granules independent of G3BP1 and 2 but does not interfere with stress-induced translational inhibition. We propose a model in which UBAP2L is an essential SG nucleator that acts upstream of G3BP1 and 2 and facilitates G3BP1 core formation and SG assembly and growth.

  • G3BP
  • UBAP2L
  • Stress granule core
  • Stress granule nucleation
  • Stress granules
Citation (ISO format)
CIRILLO, Luca et al. UBAP2L forms distinct cores that act in nucleating stress granules upstream of G3BP1. In: Current Biology, 2020, vol. 30, n° 4, p. 698–707.e6. doi: 10.1016/j.cub.2019.12.020
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Article (Published version)
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ISSN of the journal0960-9822

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