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

Jinho Seo, Su Yeon Han, Daehyeon Seong, Hyun Ji Han, Jaewhan Song

Research output: Contribution to journalReview articlepeer-review

16 Citations (Scopus)


C-terminus of heat shock protein 70 (HSP70)-interacting protein (CHIP) is an E3 ligase involved in a variety of protein homeostasis events implicated in diverse signaling pathways. Its involvement in varied and even opposite signaling circuits might be due to its hallmark signature of associating with molecular chaperones, including HSP90 and HSP70. Together, these proteins may be pivotal in implementing protein quality control. A curious and puzzling aspect of the function of CHIP is its capability to induce protein degradation via the proteasome- or lysosome-dependent pathways. In addition, these pathways are combined with ubiquitin-dependent or -independent pathways. This review focuses on the role of CHIP in the development or suppression of tumorigenesis. CHIP can act as a tumor suppressor by downregulating various oncogenes. CHIP also displays an oncogenic feature involving the inhibition of diverse tumor suppressors, including proteins related to intrinsic and extrinsic apoptotic pathways. The ability of CHIP to exhibit dual roles in determining the fate of cells has not been studied analytically. However, its association with various proteins involved in protein quality control might play a major role. In this review, the mechanistic roles of CHIP in tumor formation based on the regulation of diverse proteins are discussed.

Original languageEnglish
Pages (from-to)63-75
Number of pages13
JournalArchives of pharmacal research
Issue number1
Publication statusPublished - 2019 Jan 17

Bibliographical note

Publisher Copyright:
© 2019, The Pharmaceutical Society of Korea.

All Science Journal Classification (ASJC) codes

  • Molecular Medicine
  • Drug Discovery
  • Organic Chemistry


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