RanBP3 influences interactions between CRM1 and its nuclear protein export substrates

EMBO Reports

Volumn 2, Issue 10, 2001, Pages 926-932

  Englmeier, Ludwig ^a   Fornerod, Maarten ^b   Bischoff, F Ralf ^c   Petosa, Carlo ^d   Mattaj, Iain W ^a   Kutay, Ulrike ^e  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

^b NETHERLANDS CANCER INSTITUTE   (Netherlands)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^e ETH ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR PROTEIN; RAN PROTEIN;

ARTICLE; BINDING AFFINITY; CELL MEMBRANE PERMEABILITY; CONTROLLED STUDY; DATA ANALYSIS; EUKARYOTE; IN VITRO STUDY; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN PROTEIN INTERACTION; PROTEIN TRANSPORT;

CARRIER PROTEINS; CELL NUCLEUS; DOSE-RESPONSE RELATIONSHIP, DRUG; GLUTATHIONE TRANSFERASE; GTP PHOSPHOHYDROLASES; HELA CELLS; HUMANS; KARYOPHERINS; KINETICS; NUCLEAR PROTEINS; NUCLEOCYTOPLASMIC TRANSPORT PROTEINS; PLASMIDS; PROTEIN BINDING; RAN GTP-BINDING PROTEIN; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SUBSTRATE SPECIFICITY; TIME FACTORS;

EUKARYOTA;

EID: 0034760338     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1093/embo-reports/kve200     Document Type: Article

References (32)

1. Identification of a nuclear receptor for tRNA
2. The role of exportin-t in selective nuclear export of mature tRNAs
3. RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase
4. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking
5. RanBP1 is crucial for the release of RanGTP from importin β-related nuclear transport factors
6. Co-activation of RanGTPase and inhibition of GTP dissociation by RanGTP binding protein RanBP1
7. Structure of importin-β bound to the IBB domain of importin-α
8. Receptor mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
9. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
10. CRM1 is an export receptor for leucine-rich nuclear export signals
11. CRM1 is responsible for intracellular transport mediated by the nuclear export signal
12. Transport between the cell nucleus and the cytoplasm
13. A 41 amino acid motif in importin-α confers binding to imortin-β and hence transit into the nucleus
14. Identification of different roles for RanGDP and RanGTP in nuclear protein import
15. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
16. SAC3 may link nuclear protein export to cell cycle progression
17. Export of importin α from the nucleus is mediated by a specific nuclear transport factor
18. Identification of a tRNA-specific nuclear export receptor
19. Identification of two novel RanGTP-binding proteins belonging to the importin β superfamily
20. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
21. Coordination of tRNA nuclear export with processing of tRNA
22. Nucleocytoplasmic transport, the soluble phase
23. Human RanBP3, a group of nuclear RanGTP binding proteins
24. Transport of proteins and RNAs in and out of the nucleus
25. Disruption of the YRB2 gene retards nuclear protein export, causing a profound mitotic delay and can be rescued by overexpression of XPO1/CRM1
26. PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
27. CRM1-mediated recycling of snurportin 1 to the cytoplasm
28. Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors and nucleoporins
29. Exportin 1 (Crm1p) is an essential nuclear export factor
30. A member of the Ran-binding protein family, Yrb2p, is involved in nuclear protein export
31. Structural view of the Ran-Importin β interaction at 2.3 Å resolution
32. Identification of a signal for rapid export of proteins from the nucleus