Work

Caspase‐3 cleaved p65 fragment dampens NF‐κB‐mediated anti‐apoptotic transcription by interfering with the p65/RPS3 interaction

Year: 2015

Type: article

Abstract: Caspase-3-mediated p65 cleavage is believed to suppress nuclear factor-kappa B (NF-κB)-mediated anti-apoptotic transactivation in cells undergoing apoptosis. However, only a small percentage of p65 is cleaved during apoptosis, not in proportion to the dramatic reduction in NF-κB transactivation. Here we show that the p65(1-97) fragment generated by Caspase-3 cleavage interferes with ribosomal protein S3 (RPS3), an NF-κB "specifier" subunit, and selectively retards the nuclear translocation of RPS3, thus dampening the RPS3/NF-κB-dependent anti-apoptotic gene expression. Our findings reveal a novel cell fate determination mechanism to ensure cells undergo programed cell death through interfering with RPS3/NF-κB-conferred anti-apoptotic transcription by the fragment from partial p65 cleavage by activated Caspase-3.

Source: FEBS Letters

DOI: 10.1016/j.febslet.2015.10.019

Authors: Eric M. Wier, Kai Fu, Andrea Hodgson, Xin Sun, Fengyi Wan

Institutions: Johns Hopkins University, Sidney Kimmel Comprehensive Cancer Center

Language: English

Topic: NF-κB Signaling Pathways

Subfield: Cancer Research

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: bronze