Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
권호 표지

Roles of Heat Shock Protein gp96 in the ER Quality Control: Redundant or Unique Function?

  • Yang, Yi (Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut Health Center) ;
  • Li, Zihai (Center for Immunotherapy of Cancer and Infectious Diseases, University of Connecticut Health Center)
  • Received : 2005.10.13
  • Accepted : 2005.10.15
  • Published : 2005.10.31
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Abstract

Heat shock protein gp96 is an endoplasmic reticulum chaperone, belonging to the HSP90 family. The function of gp96 as a molecular chaperone was discovered more than 10 years ago, but its importance has been overshadowed by the brilliance of its role in immune responses. It is now clear that gp96 is instrumental in the initiation of both the innate and adaptive immunity. Recently, the roles of gp96 in protein homeostasis, as well as in cell differentiation and development, are beginning to draw more attention due to rapid development in the structural study of HSP90 and some surprising new discoveries from genetic studies of gp96. In this review, we focus on the aspect of gp96 as an ER molecular chaperone in protein maturation, peptide binding and the regulation of its activity.

Keywords

References

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