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Titolo:
Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha
Autore:
Solsbacher, J; Maurer, P; Vogel, F; Schlenstedt, G;
Indirizzi:
Univ Saarlandes, D-66421 Homburg, Germany Univ Saarlandes Homburg Germany D-66421 landes, D-66421 Homburg, Germany Max Delbruck Ctr Mol Med, D-13092 Berlin, Germany Max Delbruck Ctr Mol Med Berlin Germany D-13092 D-13092 Berlin, Germany
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 22, volume: 20, anno: 2000,
pagine: 8468 - 8479
SICI:
0270-7306(200011)20:22<8468:NAYNFI>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEAR-PORE COMPLEX; RIBOSOMAL-PROTEIN L25; RNA-BINDING PROTEIN; NUCLEOCYTOPLASMIC TRANSPORT; SACCHAROMYCES-CEREVISIAE; MOLECULAR ARCHITECTURE; LOCALIZATION SIGNALS; EXPORT; RECEPTOR; ENVELOPE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Schlenstedt, G Univ Saarlandes, D-66421 Homburg, Germany Univ Saarlandes Homburg Germany D-66421 Homburg, Germany
Citazione:
J. Solsbacher et al., "Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha", MOL CELL B, 20(22), 2000, pp. 8468-8479

Abstract

Import of proteins containing a classical nuclear localization signal (NLS) into the nucleus is mediated by importin alpha and importin beta. Srp1p, the Saccharomyces cerevisiae homologue of importin alpha, returns from the nucleus in a complex with its export factor Cse1p and with Gsp1p (yeast Ran) in its GTP-bound state. We studied the role of the nucleoporin Nup2p in the transport cycle of Srp1p. Cells lacking NUP2 show a specific defect in both NLS import and Srp1p export, indicating that Nup2p is required for efficient bidirectional transport of Srp1p across the nuclear pore complex (NPC), Nup2p is located at the nuclear side of the central gated channel of theNPC and provides a binding site for Srp1p via its amino-terminal domain. We show that Nup2p effectively releases the NLS protein from importin alpha -importin and beta and strongly binds to the importin heterodimer via Srp1p. Kap95p (importin beta) is released from this complex by a direct interaction with Gsp1p-GTP. These data suggest that besides Gsp1p, which disassembles the NLS-importin alpha -importin beta complex upon binding to Kap95p in the nucleus, Nup2p can also dissociate the import complex by binding to Srp1p. We also show data indicating that Nup1p, a relative of Nup2p, plays a similar role in termination of NLS import. Cse1p and Gsp1p-GTP release Srp1pfrom Nup2p, which suggests that the Srp1D export complex can be formed directly at the NPC. The changed distribution of Cse1p at the NPC in nup2 mutants also supports a role for Nup2p in Srp1p export from the nucleus.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 08:18:05