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한남대학교

Nat. Commun., 30 December 2024 | https://doi.org/10.1038/s41467-024-55446-w NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination

Pureum Jeon ^1,8, Hyun-Ji Ham ^1,8, Haneul Choi ^1,8, Semin Park ¹, Jae-Woo Jang ¹, Sang-Won Park ², Dong-Hyung Cho ³, Hyun-Jeong Lee ⁴, Hyun Kyu Song ⁴, Masaaki Komatsu ⁵, Dohyun Han ^6,7, Deok-Jin Jang^2,*& Jin-A Lee^1,*

¹Department of Biological Sciences and Biotechnology, College of Life Sciences and Nanotechnology, Hannam University, Daejeon, Korea.
²Department of Ecological Science, College of Ecology and Environment, Kyungpook National University, Sangju, Korea.
³School of Life Sciences, BK21 FOUR KNU Creative BioRearch Group, Kyungpook National University, Daegu 41566, Korea.
⁴Department of Life Sciences, Korea University, Seoul, Korea.
⁵Department of Physiology, Juntendo University Graduate School of Medicine, Bunkyo-ku, Tokyo, Japan.
⁶Department of Transdiciplinary Medicine, Seoul National University Hospital, Seoul, Korea.
⁷Department of Medicine, Seoul National University College of Medicine, Seoul, Korea.
⁸These authors contributed equally: Pureum Jeon, Hyun-Ji Ham, Haneul Choi.

^*Corresponding authors: correspondence to Deok-Jin Jang or Jin-A Lee

Abstract

The NS1 binding protein, known for interacting with the influenza A virus protein, is involved in RNA processing, cancer, and nerve cell growth regulation. However, its role in stress response independent of viral infections remains unclear. This study investigates NS1 binding protein’s function in regulating stress granules during oxidative stress through interactions with GABARAP subfamily proteins. We find that NS1 binding protein localizes to stress granules, interacting with core components, GABARAP proteins, and p62, a protein involved in autophagy. In cells lacking NS1 binding protein, stress granule dynamics are altered, and p62 ubiquitination is increased, suggesting impaired stress granule degradation. Overexpression of NS1 binding protein reduces p62 ubiquitination. In amyotrophic lateral sclerosis patient-derived neurons, reduced NS1 binding protein and p62 disrupt stress granule morphology. These findings identify NS1 binding protein as a negative regulator of p62 ubiquitination and a facilitator of GABARAP recruitment to stress granules, implicating it in stress granule regulation and amyotrophic lateral sclerosis pathogenesis.

논문정보

형식Research article
게재일2024년 12월 (BRIC 등록일 2024-12-31)
연구진국내(교신)+국외 연구진
분야 생명과학 > 분자생물학

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