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Titolo:
Delineation of mRNA export pathways by the use of cell-permeable peptides
Autore:
Gallouzi, IE; Steitz, JA;
Indirizzi:
Yale Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Biophys & Biochem, New Haven, CT 06536 USA Yale Univ New Haven CT USA 06536 ophys & Biochem, New Haven, CT 06536 USA
Titolo Testata:
SCIENCE
fascicolo: 5548, volume: 294, anno: 2001,
pagine: 1895 - 1901
SICI:
0036-8075(20011130)294:5548<1895:DOMEPB>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; NUCLEAR-PROTEIN EXPORT; REV ACTIVATION DOMAIN; RNA-BINDING-PROTEINS; AU-RICH ELEMENTS; MESSENGER-RNA; HNRNP A1; IN-VIVO; NUCLEOCYTOPLASMIC TRANSPORT; ANTENNAPEDIA HOMEODOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
72
Recensione:
Indirizzi per estratti:
Indirizzo: Steitz, JA Yale Univ, Sch Med, Howard Hughes Med Inst, Dept Mol Biophys & Biochem, 295 Congress Ave, New Haven, CT 06536 USA Yale Univ 295 Congress Ave New Haven CT USA 06536 CT 06536 USA
Citazione:
I.E. Gallouzi e J.A. Steitz, "Delineation of mRNA export pathways by the use of cell-permeable peptides", SCIENCE, 294(5548), 2001, pp. 1895-1901

Abstract

The transport of messenger RNAs (mRNAs) from the nucleus to the cytoplasm involves adapter proteins that bind the mRNA as well as receptor proteins that interact with the nuclear pore complex. We demonstrate the utility of cell-permeable peptides designed to interfere with interactions between potential adapter and receptor proteins to define the pathways accessed by particular mRNAs. We show that HuR, a protein implicated in the stabilization of short-lived mRNAs containing AU-rich elements (AREs), serves as an adapter for c-fos mRNA export through two pathways. One involves the HuR shuttling domain, HNS, which exhibits a heat shock-sensitive interaction with transportin 2 (Trn2); the other involves two protein ligands of HuR-pp32 and APRIL-which contain leucine-rich nuclear export signals (NES) recognized by the export receptor CRM1. Heterokaryon and in situ hybridization experiments reveal that the peptides selectively block the nucleocytoplasmic shuttling of their respective adapter proteins without perturbing the overall cellular distribution of polyadenylated mRNAs.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 12:27:55