Functions of carboxyl-terminus of Hsc70 interacting protein and its role in neurodegenerative disease.
10.3760/cma.j.issn.1003-9406.2012.04.010
- Author:
Wei-qian YAN
1
;
Jun-ling WANG
;
Bei-sha TANG
Author Information
1. Department of Neurology, Central South University, Changsha, Hunan, People's Republic of China.
- Publication Type:Journal Article
- MeSH:
Animals;
Humans;
Neurodegenerative Diseases;
genetics;
metabolism;
Protein Binding;
Protein Folding;
Proteolysis;
Ubiquitin-Protein Ligases;
genetics;
metabolism
- From:
Chinese Journal of Medical Genetics
2012;29(4):426-430
- CountryChina
- Language:Chinese
-
Abstract:
Neurodegenerative diseases are a group of chronic progressive neuronal damage disorders. The cause is unclear, most of them share a same pathological hallmark with misfold proteins accumulating in neurons. Carboxyl-terminus of Hsc70 interacting protein (CHIP) is a dual functional molecule, which has a N terminal tetratrico peptide repeat (TPR) domain that interacts with Hsc/Hsp70 complex and Hsp90 enabling CHIP to modulate the aberrant protein folding; and a C terminal U-box ubiquitin ligase domain that binds to the 26S subunit of the proteasome involved in protein degradation via ubiqutin-proteasome system. CHIP protein mediates interactions between the chaperone system and the ubiquitin-proteasome system, and plays an important role in maintaining the protein homeostasis in cells. This article reviews the molecular characteristics and physiological functions of CHIP, and its role in cellular metabolism and discusses the relationship between CHIP dysfunction and neurodegenerative diseases.
