tetano
Editor, Senior Moderator
Nat Commun
. 2024 Dec 30;15(1):10925.
doi: 10.1038/s41467-024-55446-w. NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination
Pureum Jeon[SUP] #[/SUP][SUP] 1 [/SUP], Hyun-Ji Ham[SUP] #[/SUP][SUP] 1 [/SUP], Haneul Choi[SUP] #[/SUP][SUP] 1 [/SUP], Semin Park[SUP] 1 [/SUP], Jae-Woo Jang[SUP] 1 [/SUP], Sang-Won Park[SUP] 2 [/SUP], Dong-Hyung Cho[SUP] 3 [/SUP], Hyun-Jeong Lee[SUP] 4 [/SUP], Hyun Kyu Song[SUP] 4 [/SUP], Masaaki Komatsu[SUP] 5 [/SUP], Dohyun Han[SUP] 6 7 [/SUP], Deok-Jin Jang[SUP] 8 [/SUP], Jin-A Lee[SUP] 9 [/SUP]
Affiliations
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.
. 2024 Dec 30;15(1):10925.
doi: 10.1038/s41467-024-55446-w. NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination
Pureum Jeon[SUP] #[/SUP][SUP] 1 [/SUP], Hyun-Ji Ham[SUP] #[/SUP][SUP] 1 [/SUP], Haneul Choi[SUP] #[/SUP][SUP] 1 [/SUP], Semin Park[SUP] 1 [/SUP], Jae-Woo Jang[SUP] 1 [/SUP], Sang-Won Park[SUP] 2 [/SUP], Dong-Hyung Cho[SUP] 3 [/SUP], Hyun-Jeong Lee[SUP] 4 [/SUP], Hyun Kyu Song[SUP] 4 [/SUP], Masaaki Komatsu[SUP] 5 [/SUP], Dohyun Han[SUP] 6 7 [/SUP], Deok-Jin Jang[SUP] 8 [/SUP], Jin-A Lee[SUP] 9 [/SUP]
Affiliations
- PMID: 39738171
- PMCID: PMC11686067
- DOI: 10.1038/s41467-024-55446-w
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.