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Archives of Pharmacal Research

, Volume 42, Issue 1, pp 63–75 | Cite as

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

  • Jinho Seo
  • Su Yeon Han
  • Daehyeon Seong
  • Hyun-Ji Han
  • Jaewhan SongEmail author
Review
  • 277 Downloads

Abstract

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.

Keywords

CHIP Chaperone Tumorigenesis Ubiquitination Cancer 

Notes

Acknowledgements

This work was supported by grants from Creative Research Initiative Program of NRF (2015R1A3A2066581) funded by the Ministry of Science, ICT.

Compliance with ethical standards

Conflict of interest

The authors have declared that no conflict of interest exists.

Supplementary material

12272_2018_1101_MOESM1_ESM.xlsx (21 kb)
Supplementary material 1 (XLSX 20 kb)

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© The Pharmaceutical Society of Korea 2019

Authors and Affiliations

  1. 1.Department of Biochemistry, College of Life Science and BiotechnologyYonsei UniversitySeoulKorea

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