Fbxo16 mediates degradation of NF-κB p65 subunit and inhibits inflammatory response in dendritic cells.

ABSTRACT: Activation of transcription factor NF-κB is tightly regulated by negative regulatory systems that prevent excessive inflammation leading to autoimmune diseases. We previously demonstrated that PDLIM2, a PDZ-LIM domain-containing nuclear protein, functions as a ubiquitin E3 ligase that targets the p65 subunit of NF-κB and STAT3/STAT4 transcription factors for proteasomal degradation, thus terminating immune responses in dendritic cells and CD4⁺T cells, respectively. In this study, we have demonstrated that PDLIM2 forms a ubiquitin ligase complex with Cullin 1, a scaffold protein, providing a platform consisting of complex and Skp1, an adaptor protein. Moreover, by screening using siRNA for F-box-containing proteins, we have identified Fbxo16 as a substrate-recognition receptor fo

SUBMITTER: Sugimoto-Ishige A 

PROVIDER: S-EPMC12170509 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature