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Related Experiment Videos

CHIP: a quality-control E3 ligase collaborating with molecular chaperones.

Shigeo Murata1, Tomoki Chiba, Keiji Tanaka

  • 1Department of Molecular Oncology, Tokyo Metropolitan Institute of Medical Science, 3-18-22 Honkomagome, Bunkyo-ku, 113-8613, Tokyo, Japan. smurata@rinshoken.or.jp <smurata@rinshoken.or.jp>

The International Journal of Biochemistry & Cell Biology
|April 4, 2003
PubMed
Summary

Carboxyl-terminus of Hsc70 interacting protein (CHIP) links molecular chaperones and the ubiquitin-proteasome system. This protein quality control ligase targets aberrant proteins for degradation, maintaining cellular protein homeostasis.

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Cellular protein homeostasis relies on chaperone and ubiquitin-proteasome systems for removing aberrant proteins.
  • The molecular link between these two critical systems remained elusive.
  • Carboxyl-terminus of Hsc70 interacting protein (CHIP) was identified as a co-chaperone for Hsc70.

Purpose of the Study:

  • To elucidate the role of CHIP as a molecular link between chaperone and ubiquitin-proteasome systems.
  • To discuss unresolved issues regarding CHIP's molecular mechanism and in vivo functions.
  • To highlight CHIP's function as a protein quality-control ubiquitin ligase.

Main Methods:

  • Investigated the structural domains of CHIP, including the tetratricopeptide repeat (TPR) motif and U-box domain.

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  • Examined the association of CHIP with molecular chaperones Hsc70 and Hsp90.
  • Assessed the ubiquitin ligase activity of the U-box domain.

    • Main Results:

    • CHIP possesses a TPR motif for binding Hsc70 and Hsp90.
    • CHIP's U-box domain confers ubiquitin ligase activity.
    • CHIP acts as a ubiquitin ligase, targeting chaperone-recognized aberrant proteins for proteasomal degradation.

    Conclusions:

    • CHIP serves as a crucial molecular link, integrating chaperone-mediated protein recognition with ubiquitin-proteasome system degradation.
    • CHIP functions as a key protein quality-control ubiquitin ligase in maintaining cellular protein homeostasis.
    • Further investigation is needed to fully understand CHIP's in vivo mechanisms and roles.