NS1 binding protein regulates stress granule dynamics and clearance by inhibiting p62 ubiquitination.

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 amyotroph

SUBMITTER: Jeon P 

PROVIDER: S-EPMC11686067 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature