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Titolo:
Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
Autore:
Schoenfeld, AR; Davidowitz, EJ; Burk, RD;
Indirizzi:
Yeshiva Univ Albert Einstein Coll Med, Dept Microbiol & Immunol, Bronx, NY10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 onx, NY10461 USA Yeshiva Univ Albert Einstein Coll Med, Dept Pediat, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med, Dept Epidemiol & Social Med, MarionBessin Liver Res Ctr, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein CollMed Bronx NY USA 10461 nx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med, Albert Einstein Comprehens Canc Ctr, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med Bronx NY USA 10461 nx, NY 10461 USA
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 15, volume: 97, anno: 2000,
pagine: 8507 - 8512
SICI:
0027-8424(20000718)97:15<8507:EBCPDO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
BIOLOGICALLY-ACTIVE PRODUCT; UBIQUITIN LIGASE COMPLEX; VHL GENE; GERMLINE MUTATIONS; SOMATIC MUTATIONS; PROTEIN; IDENTIFICATION; BINDING; HEMANGIOBLASTOMAS; CONJUGATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Burk, RD Yeshiva Univ Albert Einstein Coll Med, Dept Microbiol & Immunol, 1300 Morris Pk Ave, Bronx, NY 10461 USA Yeshiva Univ Albert Einstein Coll Med 1300 Morris Pk Ave Bronx NY USA 10461
Citazione:
A.R. Schoenfeld et al., "Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products", P NAS US, 97(15), 2000, pp. 8507-8512

Abstract

Inactivation of the von Hippel-Lindau (VHL) tumor suppressor gene causes the familial cancer syndrome. VHL disease, characterized by a predispositionto renal cell carcinoma and other tumor types. Loss of VHL gene function also is found in a majority of sporadic renal carcinomas. A preponderance ofthe tumor-disposing inherited missense mutations detected in VHL disease are within the elongin-binding domain of VHL. This region mediates the formation of a multiprotein VHL complex containing elongin B. elongin C. cul-2. and Rbx1. This VHL complex is thought to function as an E3 ubiquitin ligase. Here, we report that VHL proteins harboring mutations which disrupt elongin binding are unstable and rapidly degraded by the proteasome. In contrast, wild-type VHL proteins are directly stabilized by associating with both elongins B and C. In addition, elongins B and C are stabilized through theirinteractions with each other and VHL. Thus, the entire VHL/elongin complexis resistant to proteasomal degradation. Because the elongin-binding domain of VHL is frequently mutated in cancers, these results suggest that loss of elongin binding causes tumorigenesis by compromising VHL protein stability and/or potential VHL ubiquitination functions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/01/21 alle ore 08:03:13