RNF152, a novel lysosome localized E3 ligase with pro-apoptotic activities
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Updated: Jun 5, 2026

Characterization of MLKL-mediated Plasma Membrane Rupture in Necroptosis
Published on: August 7, 2018
Songling Zhang1, Wei Wu, Yanfang Wu
1Key Laboratory of Infection and Immunity of Chinese Academy of Sciences, the Institute of Biophysics, Beijing, 100101, China.
Abstract:
RING finger protein 152 (RNF152) is a novel RING finger protein and has not been well characterized. We report here that RNF152 is a canonical RING finger protein and has E3 ligase activity. It is polyubiqitinated partly through Lys-48-linked ubiquitin chains in vivo and this phenomenon is dependent on its RING finger domain and transmembrane domain. RNF152 is localized in lysosomes and co-localized with LAMP3, a lysosome marker. Moreover, over-expression of RNF152 in Hela cells induces apoptosis. These results suggest that RNF152 is a lysosome localized E3 ligase with pro-apoptotic activities. It is the first E3 ligase identified so far that is involved in lysosome-related apoptosis.
Insights
RING finger protein 152 (RNF152) is a novel E3 ligase localized in lysosomes. This protein induces apoptosis, representing the first E3 ligase identified in lysosome-related cell death pathways.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- RING finger protein 152 (RNF152) is a novel protein with limited characterization.
- E3 ubiquitin ligases play critical roles in protein degradation and cellular signaling.
- Lysosomes are key organelles involved in cellular waste disposal and signaling.
Purpose of the Study:
- To characterize the function and localization of the novel RING finger protein 152 (RNF152).
- To investigate the enzymatic activity and cellular localization of RNF152.
- To determine the role of RNF152 in apoptosis and cellular pathways.
Main Methods:
- Western blotting and immunoprecipitation to assess polyubiquitination.
- Immunofluorescence microscopy to determine subcellular localization.
- Overexpression studies in HeLa cells to evaluate apoptosis induction.
Main Results:
- RNF152 exhibits canonical RING finger protein characteristics and possesses E3 ligase activity.
- RNF152 undergoes polyubiquitination, dependent on its RING finger and transmembrane domains.
- RNF152 is localized to lysosomes and co-localizes with LAMP3, a lysosome marker.
- Overexpression of RNF152 induces apoptosis in HeLa cells.
Conclusions:
- RNF152 is a lysosome-localized E3 ligase with pro-apoptotic functions.
- This study identifies RNF152 as the first E3 ligase implicated in lysosome-related apoptosis.
- RNF152 represents a potential new target for understanding and manipulating cell death pathways.
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