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Titolo:
NUCLEAR-CYTOPLASMIC SHUTTLING OF C-ABL TYROSINE KINASE
Autore:
TAAGEPERA S; MCDONALD D; LOEB JE; WHITAKER LL; MCELROY AK; WANG JYJ; HOPE TJ;
Indirizzi:
UNIV CALIF SAN DIEGO,CTR MOL GENET,DEPT BIOL LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,CTR MOL GENET,DEPT BIOL LA JOLLA CA 92093 UNIV CALIF SAN DIEGO,CTR CANC LA JOLLA CA 92093 SALK INST BIOL STUDIES,INFECT DIS LAB LA JOLLA CA 92037
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 13, volume: 95, anno: 1998,
pagine: 7457 - 7462
SICI:
0027-8424(1998)95:13<7457:NSOCTK>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
RNA-POLYMERASE-II; VIRUS TYPE-1 REV; RETINOBLASTOMA PROTEIN FUNCTION; TERMINAL REPEATED DOMAIN; IMMUNODEFICIENCY-VIRUS; EXPORT SIGNAL; EFFECTOR DOMAINS; CELL-CYCLE; BINDING; PHOSPHORYLATION;
Keywords:
ADHESION; INTEGRINS; NUCLEAR EXPORT SIGNAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
S. Taagepera et al., "NUCLEAR-CYTOPLASMIC SHUTTLING OF C-ABL TYROSINE KINASE", Proceedings of the National Academy of Sciences of the United Statesof America, 95(13), 1998, pp. 7457-7462

Abstract

The ubiquitously expressed nonreceptor tyrosine kinase c-Abl containsthree nuclear localization signals, however, it is found in both the nucleus and the cytoplasm of proliferating fibroblasts. A rapid and transient loss of c-Abl from the nucleus is observed upon the initial adhesion of fibroblasts onto a fibronectin matrix, suggesting the possibility of nuclear export [Lewis, J,, Baskaran, R,, Taagepera, S., Schwartz, M, & Wang, J, (1996) Proc. Natl. Acad. Sci. USA 93, 15174-15179]. Here we show that the C terminus of c- Abl does indeed contain a functional nuclear export signal (NES) with the characteristic leucine-rich motif. The c-Abl NES can functionally complement an NES-defective HIV Rev protein (Rev Delta 3NI) and can mediate the nuclear export of glutathione-S-transferase. The c-Abl NES function is sensitive to the nuclear export inhibitor leptomycin B, Mutation of a single leucine (L1064A) in the c-Abl NES abrogates export function. The NES-mutated c-Abl, termed c-Abl NES(-), is localized exclusively to the nucleus. Treatment of cells with leptomycin B also leads to the nuclear accumulation of wild-type c-Abl protein. The c-Abl NES(-) is not lost from the nucleus when detached fibroblasts are replated onto fibronectin matrix, Taken together, these results demonstrate that c-Abl shuttles continuously between the nucleus and the cytoplasm and that the rate of nuclear import and export can be modulated by the adherence status of fibroblastic cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:13:36