PBLD Orchestrates the STING-Mediated Antiviral Immune Response and Autoimmune Diseases.
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ABSTRACT: Precise regulation of stimulator of interferon genes (STING) expression is critical for maintaining immune homeostasis and preventing autoimmune disorders. In this study, phenazine biosynthesis-like domain-containing protein (PBLD) is identified as a key modulator of the STING-dependent antiviral type I interferon (IFN) response by suppressing coiled-coil domain-containing protein 50 (CCDC50)-mediated selective autophagic degradation of STING. Notably, viral infection downregulates PBLD expression through two distinct mechanisms: transcriptional suppression via reduced transcription factor EB (TFEB) activity, and post-translational degradation through an enhanced membrane-associated RING finger protein 2 (MARCH2)-mediated ubiquitin-proteasome pathway. Together, these mechanisms establish a
SUBMITTER: Hou P
PROVIDER: S-EPMC12822414 | biostudies-literature | 2026 Jan
REPOSITORIES: biostudies-literature
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