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Titolo:
Interaction between RGS7 and polycystin
Autore:
Kim, E; Arnould, T; Sellin, L; Benzing, T; Comella, N; Kocher, O; Tsiokas, L; Sukhatme, VP; Walz, G;
Indirizzi:
Harvardoston, Div Renal, Beth Israel Deaconess Med Ctr, Sch Med,Dept Med, B Harvard Univ Boston MA USA 02215 l Deaconess Med Ctr, Sch Med,Dept Med, B Harvard,Univ, Div Renal, Beth Israel Deaconess Med Ctr, Sch Med,Dept Pathol Harvard Univ Boston MA USA 02215 l Deaconess Med Ctr, Sch Med,Dept Pathol Harvardon,iv, Massachusetts Gen Hosp, Sch Med, Lab Mol & Dev Neurosci, Bost Harvard Univ Boston MA USA 02114 p, Sch Med, Lab Mol & Dev Neurosci, Bost
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 11, volume: 96, anno: 1999,
pagine: 6371 - 6376
SICI:
0027-8424(19990525)96:11<6371:IBRAP>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
GTPASE-ACTIVATING PROTEIN; HETEROTRIMERIC G-PROTEINS; ALPHA-SUBUNITS; TRANSITION-STATE; MAMMALIAN-CELLS; FAMILY MEMBERS; KIDNEY-DISEASE; GAIP; DOMAIN; YEAST;
Keywords:
protein-protein interaction; yeast two-hybrid system; polycystic kidney disease;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Walz, G HarvardANAiv, Div Renal, Beth Israel Deaconess Med Ctr, Sch Med,Dept Med, D Harvard Univ DANA 517,330 Brookline Ave Boston MA USA 02215 Med, D
Citazione:
E. Kim et al., "Interaction between RGS7 and polycystin", P NAS US, 96(11), 1999, pp. 6371-6376

Abstract

Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of certain G alpha subunits and thereby modulate a number of G protein-dependent signaling cascades, Currently, little is known about the regulation of RGS proteins themselves, We identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway. Thedegradation of RGS7 is inhibited by interaction with a C-terminal domain of polycystin, the protein encoded by PKD1, a gene involved in autosomal-dominant polycystic kidney disease. Furthermore, membranous expression of C-terminal polycystin relocalized RGS7. Our results indicate that rapid degradation and interaction with integral membrane proteins are potential means ofregulating RGS proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 15:37:35