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J. Biol. Chem., Vol. 277, Issue 43, 40247-40252, October 25, 2002
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§,§,,
,, and¶**
From PTEN is a tumor suppressor that primarily
dephosphorylates phosphatidylinositol 3,4,5-trisphosphate to
down-regulate the phosphoinositide 3-kinase/Akt signaling pathway.
Although the cellular functions of PTEN as a tumor suppressor have been
well characterized, the mechanism by which PTEN activity is modulated
by other signal molecules in vivo remains poorly
understood. In searching for potential PTEN modulators through
protein-protein interaction, we identified the major vault protein
(MVP) as a dominant PTEN-binding protein in a yeast two-hybrid screen.
MVP is the major structural component of vault, the largest
intracellular ribonucleoprotein particle. Co-immunoprecipitation
confirmed the interaction between PTEN and MVP in transfected mammalian
cells. More importantly, we found that a significant portion of
endogenous PTEN associates with vault particles in human HeLa cells.
Deletion mutation analysis demonstrated that MVP binds to the C2 domain
of PTEN and that PTEN interacts with MVP through its EF
hand-like motif. Furthermore, the in vitro binding
experiments revealed that the interaction of PTEN with MVP is
Ca2+-dependent.
Mammalian Cell Genetics, Biotechnology Research
Institute, National Research Council of Canada, Montreal, Quebec H4P
2R2, Canada and ¶ Department of Medicine, McGill University,
Montreal, Quebec H3G 1A4, Canada
Current address: NuGEN Technologies, 821 Industrial Rd., Unit
A, San Carlos, CA.
**
To whom correspondence should be addressed: Health Sector,
Biotechnology Research Inst., National Research Council of
Canada, Montreal, Quebec H4P 2R2, Canada. Tel.: 514-496-6318;
Fax: 514-496-6319; E-mail: shi.shen@nrc.ca.
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