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HSP 60 overexpression increases the protein levels of the p110α subunit of phosphoinositide 3‐kinase and c‐Myc
Author(s) -
Yan FengQin,
Wang JianQiu,
Tsai YaPing,
Wu KouJuey
Publication year - 2015
Publication title -
clinical and experimental pharmacology and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.752
H-Index - 103
eISSN - 1440-1681
pISSN - 0305-1870
DOI - 10.1111/1440-1681.12457
Subject(s) - hsp60 , protein subunit , phosphoinositide 3 kinase , heat shock protein , protein kinase b , hsp90 , microbiology and biotechnology , phosphorylation , chemistry , biology , biochemistry , hsp70 , gene
Summary Heat shock protein 60 ( HSP 60) is a chaperone protein which plays an essential role in facilitating the folding of many newly synthesized proteins to reach their native forms. Increased HSP 60 expression is observed in various types of human cancers. However, proteins induced by HSP 60 to mediate transformation remain largely unknown. Here we show that HSP 60 overexpression increases the protein levels of the p110α subunit of phosphoinositide 3‐kinase ( PI 3K). The amino acid domain 288‐383 of HSP 60 is used to increase the protein levels. Overexpression of HSP 60 also induces the levels of phosphorylated Akt. In addition, the amino acid domain 288‐383 of HSP 60 is used to induce c‐Myc expression. Finally, a mono‐ubiquitinated form of β‐catenin has a higher activity to activate β‐catenin downstream targets compared to wild‐type β‐catenin. These results indicate that HSP 60 overexpression induces the levels or activity of multiple oncogenic proteins to mediate transformation.