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Updated: Jan 24, 2026
Generation and Isolation of Cell Cycle-arrested Cells with Complex Karyotypes
Published on: April 13, 2018
The Ribosomal Protein RPLP0 Mediates PLAAT4-induced Cell Cycle Arrest and Cell Apoptosis
Chun-Hua Wang1,2, Lu-Kai Wang3, Chang-Chieh Wu4
1Department of Dermatology, Taipei Tzuchi Hospital, Buddhist Tzuchi Medical Foundation, 231, New Taipei City, Taiwan.
Abstract:
Phospholipase A and acyltransferase 4 (PLAAT4) is a member of the HREV107 tumor suppressor gene family. The expression of PLAAT4 has been shown to induce cell death; however, the underlying mechanism remains unknown. Here, we found that RPLP0, a ribosomal protein, can interact with PLAAT4, as determined by yeast two-hybrid screening, coimmunoprecipitation, and colocalization. The level of RPLP0 was suppressed in HtTA cervical cancer cells expressing PLAAT4. In PLAAT4-expressing or RPLP0-silenced cells, decreased cell viability and cell proliferation combined with increased cell death were observed. Furthermore, the levels of cell cycle-associated proteins and anti-apoptotic proteins decreased in PLAAT4-expressing or RPLP0-silenced cells. Similar patterns of cell viability and expression levels of cell-cycle-associated proteins and apoptosis-related proteins were observed in PLAAT4-expressing and RPLP0-knockdown cells, indicating that RPLP0 deficiency might be involved in PLAAT4-mediated growth inhibition and cellular apoptosis.
Insights
Phospholipase A and acyltransferase 4 (PLAAT4) interacts with ribosomal protein RPLP0, suppressing its levels. This interaction leads to reduced cell viability and increased cell death, suggesting RPLP0
Area of Science:
- Molecular Biology
- Cell Biology
- Cancer Research
Background:
- Phospholipase A and acyltransferase 4 (PLAAT4) is a tumor suppressor gene.
- PLAAT4 expression induces cell death, but the mechanism is unclear.
Purpose of the Study:
- To elucidate the mechanism of PLAAT4-mediated cell death.
- To investigate the interaction between PLAAT4 and other cellular components.
Main Methods:
- Yeast two-hybrid screening
- Coimmunoprecipitation
- Colocalization studies
- Cell viability assays
- Cell proliferation assays
- Western blotting for cell cycle and apoptosis proteins
Main Results:
- RPLP0, a ribosomal protein, was identified as an interactor of PLAAT4.
- PLAAT4 expression suppressed RPLP0 levels in cervical cancer cells.
- PLAAT4 expression or RPLP0 silencing decreased cell viability and proliferation.
- PLAAT4 expression or RPLP0 silencing increased cell death.
- Levels of cell cycle-associated and anti-apoptotic proteins were reduced.
Conclusions:
- RPLP0 interacts with PLAAT4.
- RPLP0 deficiency is implicated in PLAAT4-mediated growth inhibition and apoptosis.
- PLAAT4 may regulate cell death pathways through RPLP0.
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