HSP60 overexpression increases the protein levels of the p110α subunit of  phosphoinositide 3-kinase and c-Myc

Feng Qin Yan, Jian Qiu Wang, Ya Ping Tsai*, Kou Juey Wu

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

15 Scopus citations

Abstract

Heat shock protein 60 (HSP60) is a chaperone protein which plays an essential role in facilitating the folding of many newly synthesized proteins to reach their native forms. Increased HSP60 expression is observed in various types of human cancers. However, proteins induced by HSP60 to mediate transformation remain largely unknown. Here we show that HSP60 overexpression increases the protein levels of the p110α subunit of phosphoinositide 3-kinase (PI3K). The amino acid domain 288-383 of HSP60 is used to increase the protein levels. Overexpression of HSP60 also induces the levels of phosphorylated Akt. In addition, the amino acid domain 288-383 of HSP60 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 HSP60 overexpression induces the levels or activity of multiple oncogenic proteins to mediate transformation.

Original languageEnglish
Pages (from-to)1092-1097
Number of pages6
JournalClinical and Experimental Pharmacology and Physiology
Volume42
Issue number10
DOIs
StatePublished - 01 10 2015
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2015 Wiley Publishing Asia Pty Ltd.

Keywords

  • C-Myc
  • Heat shock protein 60 (HSP60)
  • P110α
  • Transformation

Fingerprint

Dive into the research topics of 'HSP60 overexpression increases the protein levels of the p110α subunit of  phosphoinositide 3-kinase and c-Myc'. Together they form a unique fingerprint.

Cite this