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Titolo:
The structural GDP/GTP cycle of human Arf6
Autore:
Pasqualato, S; Menetrey, J; Franco, M; Cherfils, J;
Indirizzi:
CNRS, Lab Enzymol & Biochim Struct, F-91198 Gif Sur Yvette, France CNRS Gif Sur Yvette France F-91198 truct, F-91198 Gif Sur Yvette, France CNRS, Inst Pharmacol Mol & Cellulaire, F-06560 Valbonne, France CNRS Valbonne France F-06560 Mol & Cellulaire, F-06560 Valbonne, France
Titolo Testata:
EMBO REPORTS
fascicolo: 3, volume: 2, anno: 2001,
pagine: 234 - 238
SICI:
1469-221X(200103)2:3<234:TSGCOH>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUANINE-NUCLEOTIDE EXCHANGE; ADP-RIBOSYLATION FACTOR-1; GTP HYDROLYSIS; GDP; COMPLEX; MYRISTOYLATION; GTPASES; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Cherfils, J CNRS, Lab Enzymol & Biochim Struct, 1 Ave Terrasse, F-91198 Gif Sur Yvette, France CNRS 1 Ave Terrasse Gif Sur Yvette France F-91198 tte, France
Citazione:
S. Pasqualato et al., "The structural GDP/GTP cycle of human Arf6", EMBO REP, 2(3), 2001, pp. 234-238

Abstract

The small GTP-binding protein Arf6 coordinates membrane traffic at the plasma membrane with aspects of cytoskeleton organization. This function does not overlap with that of other members of the ADP-ribosylation factor (Arf)family, although their switch regions, which are their major sites of interaction with regulators and effecters, have virtually identical sequences. Here we report the crystal structure of full-length, non-myristoylated human Arf6 bound to GTP gammaS. Unlike their GDP-bound forms, the active forms of Arf6 and Arf1 are very similar. Thus, the switch regions are discriminatory elements between Arf isoforms in their inactive but not in their activeforms, a property that may generalize to other families of small G proteins. This suggests that GTP-bound Arfs may establish specific interactions outside the switch regions and/or be recognized in their cellular context rather than as isolated proteins. The structure also allows further insight into the lack of spontaneous GTPase activity of Arf proteins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 03:23:22