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Human selenium binding protein-1 (hSP56) interacts with VDU1 in a selenium-dependent manner
Jee-Yeong Jeong1, Yuxun Wang, Arthur J Sytkowski
1Laboratory for Cell and Molecular Biology, Division of Hematology and Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, 330 Brookline Avenue, Boston, MA 02215, USA.
Biochemical and Biophysical Research Communications
|January 3, 2009
Summary
Reduced expression of human selenium binding protein-1 (hSP56) is linked to cancer. This study identifies VDU1 as a binding partner, suggesting hSP56
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Reduced expression of human selenium binding protein-1 (hSP56) is observed in various cancers.
- hSP56 is implicated in selenium-dependent cell growth inhibition, but its molecular function is unclear.
Purpose of the Study:
- To identify protein partners of hSP56.
- To elucidate the molecular basis of hSP56 function in cancer.
Main Methods:
- Yeast two-hybrid screen to identify protein interactions.
- In vitro binding assays and co-localization studies in LNCaP cells.
- Analysis of selenium incorporation into hSP56.
Main Results:
- Identified von Hippel-Lindau protein (pVHL)-interacting deubiquitinating enzyme 1 (VDU1) as an hSP56 interacting partner.
- Confirmed interaction and co-localization of hSP56 and VDU1 in prostate cancer cells.
- Demonstrated selenium incorporation into hSP56, distinct from conventional selenoproteins.
Conclusions:
- hSP56 interacts with VDU1, suggesting a role in protein degradation pathways.
- Selenium-dependent function of hSP56 may involve ubiquitination/deubiquitination processes.
- Further research into hSP56 and VDU1 interactions could reveal novel cancer therapeutic targets.
