CHIP is associated with Parkin, a gene responsible for familial Parkinson's Disease, and enhances its ubiquitin ligase activity

Molecular Cell

Volumn 10, Issue 1, 2002, Pages 55-67

  Imai, Yuzuru ^a   Soda, Mariko ^a   Hatakeyama, Shigetsugu ^b,c   Akagi, Takumi ^a   Hashikawa, Tsutomu ^a   Nakayama, Kei Ichi ^b,c   Takahashi, Ryosuke ^a  

^a RIKEN BRAIN SCIENCE INSTITUTE   (Japan)

^b KYUSHU UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK PROTEIN 70; LIGASE; PAEL RECEPTOR; PARKIN; PROTEIN; PROTEIN CHIP; RECEPTOR; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CELL DEATH; CONTROLLED STUDY; DISSOCIATION; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; ENZYME REGULATION; HUMAN; HUMAN CELL; PARKINSON DISEASE;

MAMMALIA;

EID: 0036345454     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(02)00583-X     Document Type: Article

References (32)

1. Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's disease
2. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
3. The Hsp70 and Hsp60 chaperone machines
4. Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance
5. The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
6. Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms
7. Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
8. U box proteins as a new family of ubiquitin-protein ligases
9. The ubiquitin system
10. Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity
11. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
12. The lore of the RINGs: Substrate recognition and catalysis by ubiquitin ligases
13. CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
14. RING finger proteins: Mediators of ubiquitin ligase activity
15. Protein folding in vivo: Unraveling complex pathways
16. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
17. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
18. Aggresomes, inclusion bodies and protein aggregation
19. Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's disease
20. The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
21. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
22. Neurochemical and neurogenetic correlates of Parkinson's disease
23. A novel transactivation domain in parkin
24. CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
25. Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
26. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative diseases
27. Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase
28. Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70
29. Posttranslational quality control: Folding, refolding, and degrading proteins
30. Parkin immunoreactivity in the brain of human and non-human primates: An immunohistochemical analysis in normal conditions and in Parkinsonian syndromes
31. Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1
32. Proteasome inhibitor induced gene expression profiles reveal overexpression of transcriptional regulators ATF3, GADD153 and MAD1