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Titolo:
Nucleocytoplasmic shuttling by protein nuclear import factors
Autore:
Truant, R; Fridell, RA; Benson, ER; Herold, A; Cullen, BR;
Indirizzi:
Duke Univ, Med Ctr, Howard Hughes Med Inst, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 oward Hughes Med Inst, Durham, NC 27710 USA Duke Univ, Med Ctr, Dept Genet, Durham, NC 27710 USA Duke Univ Durham NC USA 27710 , Med Ctr, Dept Genet, Durham, NC 27710 USA
Titolo Testata:
EUROPEAN JOURNAL OF CELL BIOLOGY
fascicolo: 4, volume: 77, anno: 1998,
pagine: 269 - 275
SICI:
0171-9335(199812)77:4<269:NSBPNI>2.0.ZU;2-G
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSPORT FACTOR; BINDING-PROTEIN; PORE COMPLEX; HNRNP A1; BETA; INTERACTS; EXPORT; IDENTIFICATION; MIGRATION; SEQUENCE;
Keywords:
importin beta; transportin; nucleocytoplasmic shuttling; nuclear localization signal;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Cullen, BR Duke Univ, Med Ctr, Howard Hughes Med Inst, Box 3025, Durham, NC 27710 USA Duke Univ Box 3025 Durham NC USA 27710 25, Durham, NC 27710 USA
Citazione:
R. Truant et al., "Nucleocytoplasmic shuttling by protein nuclear import factors", EUR J CELL, 77(4), 1998, pp. 269-275

Abstract

Protein nuclear import factors are not, in general, believed to function in the nuclear export of macromolecules and their reutilization therefore requires their recycling from the nucleus to the cytoplasm. Two possible mechanisms for recycling have been proposed. On the one hand, protein import factors such as importin beta and transportin (Trn) could continuously shuttle between cytoplasm and nucleoplasm. On the other hand, these proteins could penetrate into the nucleus only as far as the inner surface of the nuclear pore complex and then directly return to the cytoplasm. In this manuscript, we have used microinjection analysis in human cells, and in vitro nuclear assays, to demonstrate that importin beta, transportin and importin alphaare all nucleocytoplasmic shuttle proteins that efficiently enter and exitthe cell nucleoplasm. In the case of transportin, we have mapped sequencesrequired for nucleocytoplasmic shuttling to the carboxy-terminal 270 aminoacids of this 890 amino acid import factor, thus demonstrating that nuclear export is independent of the amino-terminal Ran-binding domain of Trn. Wefurther show that Trn shuttling is independent of nuclear RNA transcription, Overall, these data suggest that nucleocytoplasmic shuttling is likely to be a general attribute of protein nuclear import factors.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 17:09:24