Fromthe ‡ DepartmentofEnvironmentalMedicineandPharmacology,NewYorkUniversitySchoolofMedicine, Tuxedo,NewYork10987,the § CellBiologyProgram,MemorialSloan-KetteringCancerCenter,NewYork,NewYork10024, andtheDepartmentofMedicine,DavidGeffenSchoolofMedicine,UCLA,Torrance, California 90502

@inproceedings{Xu2010FromtheD,
  title={Fromthe ‡ DepartmentofEnvironmentalMedicineandPharmacology,NewYorkUniversitySchoolofMedicine, Tuxedo,NewYork10987,the § CellBiologyProgram,MemorialSloan-KetteringCancerCenter,NewYork,NewYork10024, andtheDepartmentofMedicine,DavidGeffenSchoolofMedicine,UCLA,Torrance, California 90502},
  author={Da-zhong Xu and Yixin Yao and Xuejun Jiang and Lianming Lu and Wei Dai},
  year={2010}
}
By studying primary isogenic murine embryonic fibroblasts (MEFs), we have shown that PLK3 null MEFs contain a reduced level of phosphatase and tensin homolog (PTEN) and increased Akt1 activation coupled with decreased GSK3 activation under normoxia and hypoxia. Purified recombinant Plk3, but not a kinase-defective mutant, efficiently phosphorylates PTEN in vitro. Mass spectrometry identifies threonine 366 and serine 370 as two putative residues that are phosphorylated by Plk3. Immunoblotting… CONTINUE READING

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