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Titolo:
Qualitative highly divergent nuclear export signals can regulate export bythe competition for transport cofactors in vivo
Autore:
Heger, P; Lohmaier, J; Schneider, G; Schweimer, K; Stauber, RH;
Indirizzi:
Univ Erlangen Nurnberg, Inst Clin & Mol Virol, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Erlangen Germany D-91054 -91054 Erlangen, Germany Univ Bayreuth, Lehrstuhl Biopolymere, D-95440 Bayreuth, Germany Univ Bayreuth Bayreuth Germany D-95440 lymere, D-95440 Bayreuth, Germany
Titolo Testata:
TRAFFIC
fascicolo: 8, volume: 2, anno: 2001,
pagine: 544 - 555
SICI:
1398-9219(200108)2:8<544:QHDNES>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; REV-RESPONSE ELEMENT; MESSENGER-RNA EXPORT; NUCLEOCYTOPLASMIC TRANSPORT; LIVING CELLS; CYTOPLASMIC LOCALIZATION; SUBCELLULAR-LOCALIZATION; PROTEIN EXPORT; PORE COMPLEX; TYPE-1 REV;
Keywords:
CRM1; NES; nucleo-cytoplasmic transport; nucleoporins; HIV; Rev; PKI;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Stauber, RH Univ Erlangen Nurnberg, Inst Clin & Mol Virol, Schlossgarten 4, D-91054 Erlangen, Germany Univ Erlangen Nurnberg Schlossgarten 4 Erlangen Germany D-91054
Citazione:
P. Heger et al., "Qualitative highly divergent nuclear export signals can regulate export bythe competition for transport cofactors in vivo", TRAFFIC, 2(8), 2001, pp. 544-555

Abstract

Nucleo-cytoplasmic transport of proteins is mediated by nuclear export signals, identified in various proteins executing heterologous biological functions. However, the molecular mechanism underlying the orchestration of export is only poorly understood. Using microinjection of defined recombinant export substrates, we now demonstrate that leucine-rich nuclear export signals varied dramatically in determining the kinetics of export in vivo. Thus, nuclear export signals could be kinetically classified which correlated with their affinities for CRM1-containing export complexes in vitro. Strikingly, cotransfection experiments revealed that proteins containing a fast nuclear export signal inhibited export and the biological activity of proteins harboring a slower nuclear export signal in vivo. The affinity for exportcomplexes seems therefore predominantly controlled by the nuclear export signal itself, even in the context of the complete protein in vivo. Overexpression of FG-rich repeats of nucleoporins affected a medium nuclear export signal containing protein to the same extent as a fast nuclear export signal containing protein, indicating that nucleoporins appear not to contributesignificantly to nuclear export signal-specific export regulation. Our results imply a novel mode for controlling the biological activity of shuttle proteins already by the composition of the nuclear export signal itself.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 13:15:30