Two Closely Related Human Nuclear Export Factors Utilize Entirely Distinct Export Pathways

Nuclear mRNA export mediated by the human protein TAP requires a carboxy-terminal domain that directly interacts with components of the nuclear pore complex. Here we demonstrate that NXF3, a human RNA binding protein related to TAP, lacks this domain yet retains the ability to export tethered RNA tr...

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Veröffentlicht in:	Molecular cell 2001-08, Vol.8 (2), p.397-406
Hauptverfasser:	Yang, Jin, Bogerd, Hal P., Wang, P.Jeremy, Page, David C., Cullen, Bryan R.
Format:	Artikel
Sprache:	eng
Schlagworte:	Active Transport, Cell Nucleus - physiology Animals ATP Binding Cassette Transporter, Subfamily B, Member 2 ATP-Binding Cassette Transporters Binding Sites Carrier Proteins - metabolism Cell Line Cell Nucleus - metabolism Exportin 1 Protein Genes, Reporter - genetics Humans Immunoblotting Karyopherins Models, Molecular Nucleocytoplasmic Transport Proteins NXF3 protein Protein Binding Protein Sorting Signals - physiology Protein Structure, Tertiary Receptors, Cytoplasmic and Nuclear Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA, Messenger - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism TAP protein Tissue Distribution Two-Hybrid System Techniques
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