NSP6 regulates calcium overload-induced autophagic cell death and is regulated by KLHL22-mediated ubiquitination.

ABSTRACT:

Introduction

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) poses a substantial global threat. SARS-CoV-2 nonstructural proteins (NSPs) are essential for impeding the host replication mechanism while also assisting in the production and organization of new viral components. However, NSPs are not incorporated into viral particles, and their subsequent fate within host cells remains poorly understood. Additionally, their role in viral pathogenesis requires further investigation.

Objectives

This study aimed to discover the ultimate fate of NSP6 in host cells and to elucidate its role in viral pathogenesis.

Methods

We investigated the effects of NSP6 on cell death and explored the underlying mechanism; moreover, we examined the degradation mechanism of NSP6

SUBMITTER: Tao X 

PROVIDER: S-EPMC12302427 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature