Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of tap
Autore:
Schmitt, I; Gerace, L;
Indirizzi:
Scripps Res Inst, Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA ScrippsRes Inst La Jolla CA USA 92037 Cell Biol, La Jolla, CA 92037 USA Scripps Res Inst, Res Inst, Dept Mol Biol, La Jolla, CA 92037 USA Scripps Res Inst La Jolla CA USA 92037 t Mol Biol, La Jolla, CA 92037 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 45, volume: 276, anno: 2001,
pagine: 42355 - 42363
SICI:
0021-9258(20011109)276:45<42355:IVAONT>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MESSENGER-RNA EXPORT; REV ACTIVATION DOMAIN; PORE COMPLEX; PROTEIN IMPORT; LEPTOMYCIN-B; BINDING DOMAIN; POLY(A)(+) RNA; HUMAN HOMOLOG; RAN-GTP; VIRUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
66
Recensione:
Indirizzi per estratti:
Indirizzo: Gerace, L Scripps Res Inst, Res Inst, Dept Cell Biol, 10550 N Torrey PinesRd, La Jolla, CA 92037 USA Scripps Res Inst 10550 N Torrey Pines Rd La Jolla CA USA 92037 A
Citazione:
I. Schmitt e L. Gerace, "In vitro analysis of nuclear transport mediated by the C-terminal shuttle domain of tap", J BIOL CHEM, 276(45), 2001, pp. 42355-42363

Abstract

The Tap protein of higher eukaryotes is implicated in the nuclear export of type D retroviral mRNA and some cellular mRNAs. Here we have developed anin vitro assay to study nuclear export mediated by the C-terminal shuttle domain of Tap involving the rapamycin-induced attachment of this transport domain to a nuclear green fluorescent protein-containing reporter. We foundthat export by the Tap transport domain does not involve cytosolic transport factors including the GTPase Ran. The transport domain directly binds toseveral nucleoporins positioned in different regions of the nuclear pore complex. These results argue that a direct interaction of the Tap transport domain with nucleoporins is responsible for its nucleocytoplasmic translocation. We found that the karyopherin beta -related export receptor CRM1 competes with the Tap transport domain for binding to Nup214 but not for binding to Nup62 or Nup153, suggesting that the Tap and CRM1 nuclear export pathways converge at the cytoplasmic periphery of the nuclear pore complex. Because the rates of in vitro nuclear import and export by the Tap transport domain are very similar, the directionality of mRNA export mediated by Tap probably is determined by mechanisms other than simple binding of the Tap transport domain to nucleoporins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 12:29:30