title: [The multifunctionality of CHIP protein in the protein quality-control system].
abstract: Selective protein degradation depends on their quality being controlled by the cellular system, which includes chaperones involved in protein folding and two degradation systems, the proteasomal and lysosomal. CHIP (carboxyl terminus of Hsp70-interacting protein), an E3 ubiquitin ligase and co-chaperone, serves as a chaperone-degradation system interface. This article reviews the molecular characteristics of CHIP protein, the mechanism of its action, and its role in cellular metabolism and discusses how CHIP dysfunction may lead to neurodegenerative diseases.
authors.affiliation: Instytut Biologii Ogólnej i Molekularnej, Zakład Genetyki, Uniwersytet Mikołaja Kopernika w Toruniu, Toruń. rlenart@umk.pl <rlenart@umk.pl>
authors.forename: Robert
authors.initials: R
authors.lastname: Lenartowski
authors.forename: Krzysztof
authors.initials: K
authors.lastname: Gumowski
authors.forename: Anna
authors.initials: A
authors.lastname: Goc
mesh_terms: D006801:Humans; D019636:Neurodegenerative Diseases / Q000378:metabolism*; D015398:Signal Transduction; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
chemical_list: C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases