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The association of ubiquitin-associated protein 2-like and Ras-GTP-activating protein SH3 domain binding protein 1 mediated by small nucleolar RNA is essential for stress granule formation

Eri Asano-Inami, Akira Yokoi, Mai Sugiyama, Toshinori Hyodo, Tomonari Hamaguchi, Hiroaki Kajiyama
doi: https://doi.org/10.1101/2022.04.20.488692
Eri Asano-Inami
1Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
2Bell Research Center for Reproductive Health and Cancer; Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
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  • For correspondence: eri-inami@kishokai.or.jp ayokoi@med.nagoya-u.ac.jp
Akira Yokoi
1Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
3Institute for Advanced Research, Nagoya University, Nagoya, Japan
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  • For correspondence: eri-inami@kishokai.or.jp ayokoi@med.nagoya-u.ac.jp
Mai Sugiyama
2Bell Research Center for Reproductive Health and Cancer; Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
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Toshinori Hyodo
4Department of Biochemistry, Aichi Medical University School of Medicine, Nagakute, Aichi, 480-1195 Japan
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Tomonari Hamaguchi
5Division of Neurogenetics, Center for Neurological Diseases and Cancer, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
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Hiroaki Kajiyama
1Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, 65 Tsurumai-cho, Showa-ku Nagoya, 466-8550 Japan
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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 novel 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 a novel SG component, the UBAP2L/snoRNA/G3BP1 protein-RNA complex, and provide new insights into the regulation of SG assembly.

Competing Interest Statement

The authors have declared no competing interest.

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Posted April 20, 2022.
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The association of ubiquitin-associated protein 2-like and Ras-GTP-activating protein SH3 domain binding protein 1 mediated by small nucleolar RNA is essential for stress granule formation
Eri Asano-Inami, Akira Yokoi, Mai Sugiyama, Toshinori Hyodo, Tomonari Hamaguchi, Hiroaki Kajiyama
bioRxiv 2022.04.20.488692; doi: https://doi.org/10.1101/2022.04.20.488692
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The association of ubiquitin-associated protein 2-like and Ras-GTP-activating protein SH3 domain binding protein 1 mediated by small nucleolar RNA is essential for stress granule formation
Eri Asano-Inami, Akira Yokoi, Mai Sugiyama, Toshinori Hyodo, Tomonari Hamaguchi, Hiroaki Kajiyama
bioRxiv 2022.04.20.488692; doi: https://doi.org/10.1101/2022.04.20.488692

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