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Cytoplasmic localization of programmed cell death 4 contributes to its anti-apoptotic function
1Department of Biological Sciences, Graduate School of Science and Technology, Kumamoto University, 2-39-1 Kurokami, Chuo-ku, Kumamoto, 860-8555, Japan.
Molecular and Cellular Biochemistry
|February 15, 2018
Summary
Programmed cell death 4 (Pdcd4) loss triggers apoptosis. Cytoplasmic Pdcd4 localization suppresses target mRNA translation and prevents apoptosis in normal cells, revealing its anti-apoptotic role.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- Programmed cell death 4 (Pdcd4) is a known translation inhibitor.
- The precise mechanisms, timing, and location of Pdcd4's decrease during apoptosis and its anti-apoptotic function in normal cells remain unclear.
Purpose of the Study:
- To investigate the spatiotemporal dynamics of Pdcd4 during apoptosis.
- To elucidate the role of Pdcd4 localization in regulating apoptosis and translation.
Main Methods:
- Observational analysis of endogenous Pdcd4 localization in surviving and apoptotic cells.
- Treatment with leptomycin B to block nuclear export of Pdcd4.
- Overexpression of Pdcd4 to assess its effect on apoptosis and target gene expression.
Main Results:
- Endogenous Pdcd4 is found in both cytoplasm and nucleus of surviving cells.
- Nuclear Pdcd4 is lost faster than cytoplasmic Pdcd4 during apoptosis induction.
- Blocked nuclear export of Pdcd4 leads to its accumulation in the cytoplasm, reducing apoptosis.
- Overexpression of Pdcd4 suppresses Procaspase-3 translation and decreases apoptosis incidence.
Conclusions:
- Pdcd4's cytoplasmic localization is crucial for suppressing target mRNA translation and inhibiting apoptosis.
- The spatiotemporal dynamics of Pdcd4, particularly its cytoplasmic presence, dictate its anti-apoptotic function.
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