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Titolo:
E3 ubiquitin-protein ligase activity of Parkin is dependent on cooperativeinteraction of RING finger (TRIAD) elements
Autore:
Rankin, CA; Joazeiro, CAP; Floor, E; Hunter, T;
Indirizzi:
Univ Kansas, Higuchi Biosci Ctr, Lawrence, KS 66045 USA Univ Kansas Lawrence KS USA 66045 uchi Biosci Ctr, Lawrence, KS 66045 USA Univ Kansas, Mol Biosci Dept, Lawrence, KS 66045 USA Univ Kansas LawrenceKS USA 66045 Mol Biosci Dept, Lawrence, KS 66045 USA Novartis Res Fdn, Genom Inst, San Diego, CA USA Novartis Res Fdn San Diego CA USA Res Fdn, Genom Inst, San Diego, CA USA Salk Inst, Mol Biol & Virol Lab, La Jolla, CA USA Salk Inst La Jolla CA USA k Inst, Mol Biol & Virol Lab, La Jolla, CA USA
Titolo Testata:
JOURNAL OF BIOMEDICAL SCIENCE
fascicolo: 5, volume: 8, anno: 2001,
pagine: 421 - 429
SICI:
1021-7770(200109)8:5<421:EULAOP>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
RECESSIVE JUVENILE PARKINSONISM; GENE; MUTATIONS; DISEASE; DOMAINS; SYSTEM; FAMILY;
Keywords:
Parkin; Parkinson's disease; proteasome; RING finger; TRIAD/RIR domain;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Rankin, CA Univ Kansas, Higuchi Biosci Ctr, 5057 Haworth Hall, Lawrence, KS 66045 USA Univ Kansas 5057 Haworth Hall Lawrence KS USA 66045 S 66045 USA
Citazione:
C.A. Rankin et al., "E3 ubiquitin-protein ligase activity of Parkin is dependent on cooperativeinteraction of RING finger (TRIAD) elements", J BIOMED SC, 8(5), 2001, pp. 421-429

Abstract

The parkin gene codes for a 465-amino acid protein which, when mutated, results in autosomal recessive juvenile parkinsonism (AR-JP). Symptoms of AR-JP are similar to those of idiopathic Parkinson's disease, with the notableexception being the early onset of AR-JP. We have cloned and expressed human Parkin in Escherichia coli and have examined Parkin-mediated ubiquitination in an in vitro ubiquitination assay using purified recombinant proteins. We found that Parkin has E3 ubiquitin ligase activity in this system, demonstrating for the first time that the E3 activity is an intrinsic functionof the Parkin protein and does not require posttranslational modification or association with cellular proteins other than an E2 (human Ubc4 E2 was utilized in this ubiquitination assay). Mutagenesis of individual elements of the conserved RING TRIAD domain indicated that at least two elements wererequired for ubiquitin ligase activity and suggested a functional cooperation between the RING finger elements. Since the activity assays were conducted with recombinant proteins purified from E. coli, this is the first timeTRIAD element interaction has been demonstrated as an intrinsic feature ofParkin E3 activity. Copyright (C) 2001 National Science Council, ROC and S. Karger AG, Basel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/06/19 alle ore 18:00:07