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Titolo:
DETERMINATION OF THE FUNCTIONAL DOMAIN ORGANIZATION OF THE IMPORTIN-ALPHA NUCLEAR IMPORT FACTOR
Autore:
HEROLD A; TRUANT R; WIEGAND H; CULLEN BR;
Indirizzi:
DUKE UNIV,MED CTR,DEPT GENET,ROOM 426 CARL BLDG,RES DR,BOX 3025 DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT GENET DURHAM NC 27710 DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710
Titolo Testata:
The Journal of cell biology
fascicolo: 2, volume: 143, anno: 1998,
pagine: 309 - 318
SICI:
0021-9525(1998)143:2<309:DOTFDO>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
LOCALIZATION SEQUENCE RECEPTOR; REV ACTIVATION DOMAIN; PROTEIN IMPORT; HUMAN HOMOLOG; CELLULAR COFACTOR; TRANSPORT FACTORS; EXPORT SIGNAL; IDENTIFICATION; INTERACTS; BINDING;
Keywords:
IMPORTIN ALPHA; NUCLEAR EXPORT; NUCLEAR IMPORT; NUCLEAR LOCALIZATION SIGNAL;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
48
Recensione:
Indirizzi per estratti:
Citazione:
A. Herold et al., "DETERMINATION OF THE FUNCTIONAL DOMAIN ORGANIZATION OF THE IMPORTIN-ALPHA NUCLEAR IMPORT FACTOR", The Journal of cell biology, 143(2), 1998, pp. 309-318

Abstract

Although importin alpha (Imp alpha) has been shown to act as the receptor for basic nuclear localization signals (NLSs) and to mediate their recruitment to the importin beta nuclear import factor, little is known about the functional domains present in Imp alpha, with the exception that importin beta binding is known to map close to the Imp alpha NH2 terminus. Here, we demonstrate that sequences essential for binding to the CAS nuclear export factor are located near the Imp alpha COOHterminus and include a critical acidic motif. Although point mutations introduced into this acidic motif inactivated both CAS binding and Imp alpha nuclear export, a putative leucine-rich nuclear export signalproved to be neither necessary nor sufficient for Imp alpha nuclear export. Analysis of sequences within Imp alpha that bind to the SV-40 Tantigen NLS or to the similar LEF-1 NLS revealed that both NLSs interact with a subset of the eight degenerate armadillo (Arm) repeats thatform the central part of Imp a. However, these two NLS-binding sites showed only minimal overlap, thus suggesting that the degeneracy of the Arm repeat region of Imp alpha may serve to facilitate binding to similar but nonidentical basic NLSs. Importantly, the SV-40 TNLS proved able to specifically inhibit the interaction of Imp alpha with CAS in vitro, thus explaining why the SV-40 T NLS is unable to also function as a nuclear export signal.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/09/20 alle ore 12:01:27