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Multifaceted C-terminus of HSP70-interacting protein regulates tumorigenesis via protein quality control

Jinho Seo1, Su Yeon Han1, Daehyeon Seong1

  • 1Department of Biochemistry, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, Korea.

Archives of Pharmacal Research
|January 3, 2019
PubMed

Insights

Heat shock protein 70 (HSP70)-interacting protein (CHIP) regulates protein homeostasis and has dual roles in cancer, acting as both a tumor suppressor and oncogene by affecting protein degradation pathways.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Oncology

Background:

  • C-terminus of HSP70-interacting protein (CHIP) is an E3 ligase crucial for protein homeostasis.
  • CHIP interacts with molecular chaperones like HSP90 and HSP70, influencing protein quality control.
  • CHIP's function in protein degradation via proteasomal or lysosomal pathways is complex.

Purpose of the Study:

  • To review the dual role of CHIP in tumorigenesis.
  • To discuss the mechanistic roles of CHIP in tumor development and suppression.
  • To analyze CHIP's involvement in regulating oncogenes and tumor suppressors.

Main Methods:

  • Literature review focusing on CHIP's function in protein homeostasis and cancer.
  • Analysis of CHIP's interactions with chaperones and its role in protein degradation pathways.
  • Examination of CHIP's impact on oncogenes and tumor suppressors in various signaling pathways.

Main Results:

  • CHIP can function as a tumor suppressor by downregulating oncogenes.
  • CHIP can also act as an oncogene by inhibiting tumor suppressors, including those in apoptotic pathways.
  • CHIP's dual role is linked to its involvement in diverse protein quality control mechanisms.

Conclusions:

  • CHIP exhibits a context-dependent dual role in tumorigenesis, acting as either a tumor suppressor or an oncogene.
  • Understanding CHIP's regulation of protein degradation and its interactions with chaperones is key to deciphering its role in cancer.
  • Further analytical studies are needed to fully elucidate CHIP's complex mechanisms in cell fate determination during tumor formation.
Keywords:
CHIPCancerChaperoneTumorigenesisUbiquitination

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