Mutations in tap uncouple RNA export activity from translocation through the nuclear pore complex

• Published in: Molecular biology of the cell Vol. 17; no. 2; pp. 931 - 943
• Main Authors: Lévesque, Lyne, Bor, Yeou-Cherng, Matzat, Leah H, Jin, Li, Berberoglu, Stephen, Rekosh, David, Hammarskjöld, Marie-Louise, Paschal, Bryce M
• Format: Journal Article
• Language: English
• Published: United States The American Society for Cell Biology 01.02.2006
• Subjects: Active Transport, Cell Nucleus; Animals; ATP-Binding Cassette Transporters; Binding Sites; Cell Fusion; Cercopithecus aethiops; COS Cells; Histocompatibility Antigens Class I - chemistry; Histocompatibility Antigens Class I - genetics; Histocompatibility Antigens Class I - physiology; Humans; Mice; Mutation; NIH 3T3 Cells; Nuclear Pore - metabolism; Nucleocytoplasmic Transport Proteins - metabolism; Protein Structure, Tertiary - physiology; RNA Transport; RNA, Messenger - metabolism

Interactions between transport receptors and phenylalanine-glycine (FG) repeats on nucleoporins drive the translocation of receptor-cargo complexes through nuclear pores. Tap, a transport receptor that mediates nuclear export of cellular mRNAs, contains a UBA-like and NTF2-like folds that can associ...