
The phosphatase and tensin homolog deleted on chromosome 10 (PTEN) is a tumor-suppressing lipid phosphatase that is frequently absent in breast tumors. Thus, the stability of PTEN is essential for tumor prevention and therapy. The ubiquitin-proteasome pathway has an important role in regulating the functions of PTEN. Specifically, carboxyl terminus Hsp70-interacting protein (CHIP), the E3 ubiquitin ligase of PTEN, can regulate PTEN levels. In this study, we report that BCL-2-associated athanogene 5 (BAG5), a known inhibitor of CHIP activity, reduces the degradation of PTEN and maintains its levels via an ubiquitylation-dependent pathway. BAG5 is identified as an antagonist of cell tumorigenicity.
PTEN, CHIP, Ubiquitin, QH301-705.5, Tumor Necrosis Factor-alpha, BAG5, Ubiquitination, PTEN Phosphohydrolase, QD415-436, Biochemistry, Tissue Plasminogen Activator, Plasminogen Activator Inhibitor 1, Human Umbilical Vein Endothelial Cells, MCF-7 Cells, Prothrombin Time, Humans, Biology (General), Research Articles, Cells, Cultured, Adaptor Proteins, Signal Transducing
PTEN, CHIP, Ubiquitin, QH301-705.5, Tumor Necrosis Factor-alpha, BAG5, Ubiquitination, PTEN Phosphohydrolase, QD415-436, Biochemistry, Tissue Plasminogen Activator, Plasminogen Activator Inhibitor 1, Human Umbilical Vein Endothelial Cells, MCF-7 Cells, Prothrombin Time, Humans, Biology (General), Research Articles, Cells, Cultured, Adaptor Proteins, Signal Transducing
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