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HSP60 interacts with YB-1 and affects its polysome association and subcellular localization
Sachiyo Ohashi1, Megumi Atsumi, Shunsuke Kobayashi
1Research Unit of Biochemistry, College of Pharmacy, Nihon University, Narashinodai, Funabashi, Chiba 274-8555, Japan.
Biochemical and Biophysical Research Communications
|May 28, 2009
Summary
Heat shock protein 60 (HSP60) regulates the location of Y-box binding protein 1 (YB-1). HSP60 binds YB-1, controlling its movement between the cytoplasm and nucleus, impacting translation and cancer induction.
Area of Science:
- Molecular Biology
- Cell Biology
- Cancer Research
Background:
- Y-box binding protein 1 (YB-1) is a DNA/RNA-binding protein regulating translation via cytoplasmic polysome association.
- Nuclear accumulation of YB-1 correlates with cancer induction, suggesting a role beyond cytoplasmic translation regulation.
Purpose of the Study:
- To investigate the role of a novel nuclear localization signal (YB-NLS) in YB-1's subcellular distribution.
- To identify proteins interacting with YB-1 and regulating its nuclear translocation and polysome association.
Main Methods:
- Site-directed mutagenesis to delete the YB-NLS sequence in YB-1.
- Overexpression and repression of Heat Shock Protein 60 (HSP60) in NG108-15 cells.
- Sucrose gradient ultracentrifugation to analyze polysome association of YB-1.
Main Results:
- The YB-NLS sequence is essential for the nuclear translocation of overexpressed YB-1.
- Heat shock protein 60 (HSP60) binds to YB-1 at the YB-NLS region in the cytoplasm.
- HSP60 regulates YB-1's association with polysomes; HSP60 repression increases polysome-associated YB-1, while HSP60 overexpression decreases it.
Conclusions:
- HSP60 acts as a cytoplasmic regulator of YB-1, influencing its polysome association and subcellular distribution via the YB-NLS.
- Understanding the HSP60-YB-1 interaction provides insights into YB-1's role in translation regulation and potential involvement in cancer development.
