Görlich D, Kutay U: Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol. 1999, 15: 607-660. 10.1146/annurev.cellbio.15.1.607. A comprehensive review on nucleocytoplasmic transport, which describes the role of importins, exportins and Ran in nuclear transport and contains many references to the original work and other reviews.
Article
PubMed
Google Scholar
Kutay U, Hartmann E, Treichel N, Calado A, Carmo-Fonseca M, Prehn S, Kraft R, Görlich D, Bischoff FR: Identification of two novel RanGTP-binding proteins belonging to the importin {beta} superfamily. J Biol Chem. 2000, 275: 40163-40168. 10.1074/jbc.M006242200. Using affinity chromatography with immobilized RanGTP the authors isolate RanBP16. Another close homolog, RanBP17, is also identified on the basis of RanBP16 sequence.
Article
PubMed
CAS
Google Scholar
Plafker SM, Macara IG: Importin-11, a nuclear import receptor for the ubiquitin-conjugating enzyme, UbcM2. EMBO J. 2000, 19: 5502-5513. 10.1093/emboj/19.20.5502. This paper identifies importin 11, a human member of the importin-β family that mediates the nuclear import of UbcM2, an E2 ubiquitin-conjugating enzyme.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kutay U, Izaurralde E, Bischoff FR, Mattaj IW, Görlich D: Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. EMBO J. 1997, 16: 1153-1163. 10.1093/emboj/16.6.1153. The authors analyze the interaction sites of importin β with its multiple partners. These data suggest that termination of import involves binding of RanGTP to importin β.
Article
PubMed
CAS
PubMed Central
Google Scholar
Chi NC, Adam SA: Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore. Mol Biol Cell. 1997, 8: 945-956. The authors map the binding domains of importin β with the pore and the NLS receptor using deletion analysis and site-directed mutagenesis.
Article
PubMed
CAS
PubMed Central
Google Scholar
Cingolani G, Petosa C, Weis K, Muller CW: Structure of importin-beta bound to the IBB domain of importin-alpha. Nature. 1999, 399: 221-229. 10.1038/20367. The authors describe the crystal structure of full-length human importin β bound to the IBB domain of importin α.
Article
PubMed
CAS
Google Scholar
Chook YM, Blobel G: Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature. 1999, 399: 230-237. 10.1038/20375. This paper describes the crystal structure of full-length karyopherin β2 (transportin) bound to RanGTP. In the complex, RanGTP shows extensive structural rearrangements compared with the GDP-bound form.
Article
PubMed
CAS
Google Scholar
Vetter IR, Arndt A, Kutay U, Görlich D, Wittinghofer A: Structural view of the Ran-importin beta interaction at 2.3 A resolution. Cell. 1999, 97: 635-646. This paper reports the three-dimensional structure of a complex between Ran bound to GTP and an amino-terminal 462-residue fragment of importin β.
Article
PubMed
CAS
Google Scholar
Bayliss R, Littlewood T, Stewart M: Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell. 2000, 102: 99-108. The authors describe the crystal structure of a complex formed between residues 1-442 of importin β and the FxFG repeats from the nucleoporin Nsp1. From this information they engineer a point mutation in importin β that impairs binding to FxFG nucleoporins and decreases nuclear import in vitro.
Article
PubMed
CAS
Google Scholar
Lee SJ, Imamoto N, Sakai H, Nakagawa A, Kose S, Koike M, Yamamoto M, Kumasaka T, Yoneda Y, Tsukihara T: The adoption of a twisted structure of importin-beta is essential for the protein-protein interaction required for nuclear transport. J Mol Biol. 2000, 302: 251-264. 10.1006/jmbi.2000.4055. The authors report the crystal structure of the free amino-terminal fragment of mouse importin β. Structural analysis reveals flexible movement and rearrangements of importin β.
Article
PubMed
CAS
Google Scholar
Groves MR, Hanlon N, Turowski P, Hemmings BA, Barford D: The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell. 1999, 96: 99-110. The authors report the crystal structure of the human PR65/A subunit, revealing a left-handed superhelical conformation distinct from the right-handed superhelical fold found in importin β.
Article
PubMed
CAS
Google Scholar
Nakielny S, Dreyfuss G: Transport of proteins and RNAs in and out of the nucleus. Cell. 1999, 99: 677-690. This comprehensive review covers a large body of information, including details on cargoes, transporters and models of translocation through the NPC.
Article
PubMed
CAS
Google Scholar
Radu A, Moore MS, Blobel G: The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell. 1995, 81: 215-222. The authors report the characterization of the nucleoporin Nup98, which is located at the nucleoplasmic side of the NPC, and map an importin-β-docking site at the amino-terminal half of Nup98.
Article
PubMed
CAS
Google Scholar
Rexach M, Blobel G: Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 1995, 83: 683-692. Using a solution binding assay the authors characterize the RanGTP-induced dissociation of importin α and β and analyze the dynamics of interactions between nucleoporins and soluble transport factors bound to their cargoes.
Article
PubMed
CAS
Google Scholar
Shah S, Tugendreich S, Forbes D: Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J Cell Biol. 1998, 141: 31-49. 10.1083/jcb.141.1.31. This work shows that importin β co-purifies with Nup153 and Tpr, but not with p62, Nup93, Nup98 or Nup214. Importin β is shown to bind Nup153 directly.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kehlenbach RH, Dickmanns A, Kehlenbach A, Guan T, Gerace L: A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export. J Cell Biol. 1999, 145: 645-657. 10.1083/jcb.145.4.645. An in vitro assay is used to identify cytosolic factors required for Crm1-mediated protein export. Reconstitution experiments demonstrate that RanBP1 and the homologous domains of Nup358/RanBP2 are capable of dissociating Crm1 from the NPC.
Article
PubMed
CAS
PubMed Central
Google Scholar
Seedorf M, Damelin M, Kahana J, Taura T, Silver PA: Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol. 1999, 19: 1547-1557. Immunoprecipitation of several nuclear receptor-GFP fusions from yeast extracts show an overlapping but not identical pattern of interactions with different Nups. Pse1p-Nup interactions are shown to be dependent on the nucleotide-bound state of Ran.
Article
PubMed
CAS
PubMed Central
Google Scholar
Damelin M, Silver PA: Mapping interactions between nuclear transport factors in living cells reveals pathways through the nuclear pore complex. Mol Cell. 2000, 5: 133-140. Interactions between Nups and importins are investigated in vivo using fluorescence resonance energy transfer (FRET) in S. cerevisiae. Different variants of GFP fused to Nups and the transport factors Pse1p/Kap121p or Msn5p reveal differences in the translocation pathways.
Article
PubMed
CAS
Google Scholar
Dingwall C, Laskey RA: Nuclear targeting sequences - a consensus?. Trends Biochem Sci. 1991, 16: 478-481. 10.1016/0968-0004(91)90184-W. An overview of nuclear targeting sequences. This review provides the first description of a consensus for a bipartite NLS motif.
Article
PubMed
CAS
Google Scholar
Adam EJ, Adam SA: Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J Cell Biol. 1994, 125: 547-555. The authors describe the purification of a factor that is required to reconstitute the first step in nuclear transport, binding to the pore complex.
Article
PubMed
CAS
Google Scholar
Adam SA, Gerace L: Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import. Cell. 1991, 66: 837-847. Two polypeptides of 54 and 56 kDa were purified from bovine erythrocytes and found to bind specifically to the NLS of SV40 large T antigen.
Article
PubMed
CAS
Google Scholar
Görlich D, Vogel F, Mills AD, Hartmann E, Laskey RA: Distinct functions for the two importin subunits in nuclear protein import. Nature. 1995, 377: 246-248. 10.1038/377246a0. An importin α-importin β-import substrate complex is shown to dock to the NPC via importin β. Then, Ran-mediated translocation through the pore results in the accumulation of import substrate and importin α in the nucleus. In contrast, importin β was found to accumulate at the nuclear envelope, not in the nucleoplasm.
Article
PubMed
Google Scholar
Imamoto N, Shimamoto T, Kose S, Takao T, Tachibana T, Matsubae M, Sekimoto T, Shimonishi Y, Yoneda Y: The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile. FEBS Lett. 1995, 368: 415-419. 10.1016/0014-5793(95)00699-A. In this study, the authors cloned a cDNA encoding a 97 kDa protein of the nuclear pore-targeting complex (PTAC; identical to importin β). PTAC97 was found to reconstitute the nuclear-binding step in conjunction with a 58 kDa component of PTAC (PTAC58/importin α).
Article
PubMed
CAS
Google Scholar
Weis K, Mattaj IW, Lamond AI: Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science. 1995, 268: 1049-1053. This work describes hSRP1 alpha (importin α), which binds specifically to proteins containing either a simple or bipartite NLS motif. The hSRP1 alpha protein is shown to promote docking of import substrates to the pore and, together with Ran, to reconstitute nuclear protein import.
Article
PubMed
CAS
Google Scholar
Huber J, Cronshagen U, Kadokura M, Marshallsay C, Wada T, Sekine M, Luhrmann R: Snurportin1, an m3G-cap-specific nuclear import receptor with a novel domain structure. EMBO J. 1998, 17: 4114-4126. 10.1093/emboj/17.14.4114. Snurportin1 was identifed and found to function as an snRNP import receptor by binding m3G-cap-containing RNAs. Snurportin1 enhances cap-dependent nuclear import of U snRNPs and functions as an adaptor-like protein that interacts with importin β through an IBB domain.
Article
PubMed
CAS
PubMed Central
Google Scholar
Jullien D, Görlich D, Laemmli UK, Adachi Y: Nuclear import of RPA in Xenopus egg extracts requires a novel protein XRI-Palpha but not importin alpha. EMBO J. 1999, 18: 4348-4358. 10.1093/emboj/18.15.4348. By using a yeast two-hybrid screen, the authors identified XRIPα, which interacts with the largest subunit RPA and is required for its nuclear import. This work suggests that XRIPα serves as an adaptor to link RPA to importin β.
Article
PubMed
CAS
PubMed Central
Google Scholar
Jakel S, Albig W, Kutay U, Bischoff FR, Schwamborn K, Doenecke D, Görlich D: The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1. EMBO J. 1999, 18: 2411-2423. 10.1093/emboj/18.9.2411. Importin β and importin 7 (Imp7, RanBP7) are shown to play a critical role in nuclear import of the linker histone H1. Individually, the import receptors bind H1 weakly, but binding is strong for the heterodimer.
Article
PubMed
CAS
PubMed Central
Google Scholar
Tiganis T, Flint AJ, Adam SA, Tonks NK: Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97. J Biol Chem. 1997, 272: 21548-21557. 10.1074/jbc.272.34.21548. The nuclear-import factor p97 (importin β) is shown to bind directly to T-cell protein tyrosine phosphatase (TCPTP) and, in a permeabilized cell assay, was found to be necessary for its nuclear import.
Article
PubMed
CAS
Google Scholar
Truant R, Cullen BR: The arginine-rich domains present in human immunodeficiency virus type 1 Tat and Rev function as direct importin beta-dependent nuclear localization signals. Mol Cell Biol. 1999, 19: 1210-1217. This study defines a novel class of arginine-rich NLSs that are direct targets for importin β and function independently of importin α.
Article
PubMed
CAS
PubMed Central
Google Scholar
Palmeri D, Malim MH: Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha. Mol Cell Biol. 1999, 19: 1218-1225. The arginine-rich NLS of the Rex protein of human T-cell leukemia virus type 1 is shown to use importin β for import but does so via a mechanism which is importin-α-independent.
Article
PubMed
CAS
PubMed Central
Google Scholar
Jakel S, Görlich D: Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. EMBO J. 1998, 17: 4491-4502. 10.1093/emboj/17.15.4491. Nuclear import of ribosomal proteins is mediated by several importin-β-like transport factors, which function in the absence of importin α.
Article
PubMed
CAS
PubMed Central
Google Scholar
Moore JD, Yang J, Truant R, Kornbluth S: Nuclear import of Cdk/cyclin complexes: identification of distinct mechanisms for import of Cdk2/cyclin E and Cdc2/cyclin B1. J Cell Biol. 1999, 144: 213-224. 10.1083/jcb.144.2.213. Cyclin E and cyclin B1 are demonstrated to be imported into nuclei via distinct mechanisms. Cyclin E behaves like a classical NLS-containing protein and binds to importin α, wheras cyclin B1 is imported into the nucleus via a direct interaction with importin β.
Article
PubMed
CAS
PubMed Central
Google Scholar
Takizawa CG, Weis K, Morgan DO: Ran-independent nuclear import of cyclin B1-Cdc2 by importin beta. Proc Natl Acad Sci USA. 1999, 96: 7938-7943. 10.1073/pnas.96.14.7938. Importin β promotes cyclin B1 import in the absence of cytosol or Ran and in the presence of a dominant-negative Ran mutant.
Article
PubMed
CAS
PubMed Central
Google Scholar
Xiao Z, Liu X, Lodish HF: Importin beta mediates nuclear translocation of Smad 3. J Biol Chem. 2000, 275: 23425-23428. 10.1074/jbc.C000345200. Smad 3 binds directly to importin β.
Article
PubMed
CAS
Google Scholar
Lam MH, Briggs LJ, Hu W, Martin TJ, Gillespie MT, Jans DA: Importin beta recognizes parathyroid hormone-related protein with high affinity and mediates its nuclear import in the absence of importin alpha. J Biol Chem. 1999, 274: 7391-7398. 10.1074/jbc.274.11.7391. Importin β mediates nuclear import of parathyroid-hormone-related protein in the absence of importin α.
Article
PubMed
CAS
Google Scholar
Rout MP, Blobel G, Aitchison JD: A distinct nuclear import pathway used by ribosomal proteins. Cell. 1997, 89: 715-725. The previously uncharacterized yeast beta karyopherin Kap123p is shown to be involved in the import of ribosomal proteins into the nucleus, and the related protein Pse1p has a partially redundant function in that pathway.
Article
PubMed
CAS
Google Scholar
Schlenstedt G, Smirnova E, Deane R, Solsbacher J, Kutay U, Görlich D, Ponstingl H, Bischoff FR: Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleus. EMBO J. 1997, 16: 6237-6249. 10.1093/emboj/16.20.6237. The identification of Yrb4p (Kap123p), a protein related to importin β. Cells disrupted for YRB4 were found to be defective in nuclear import of ribosomal protein L25.
Article
PubMed
CAS
PubMed Central
Google Scholar
Aitchison JD, Blobel G, Rout MP: Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science. 1996, 274: 624-627. 10.1126/science.274.5287.624. The yeast karyopherin Kap104p was found to mediate nuclear import of two mRNA-binding proteins, Nab2p and Nab4p.
Article
PubMed
CAS
Google Scholar
Pollard VW, Michael WM, Nakielny S, Siomi MC, Wang F, Dreyfuss G: A novel receptor-mediated nuclear protein import pathway. Cell. 1996, 86: 985-994. The authors identified a 90 kDa protein, transportin, which is related to importin β. Transportin was found to mediate nuclear import of proteins containing an M9-type NLS.
Article
PubMed
CAS
Google Scholar
Fridell RA, Truant R, Thorne L, Benson RE, Cullen BR: Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta. J Cell Sci. 1997, 110: 1325-1331. The identification of a human protein related to importin β, termed MIP (transportin), which binds the M9 sequence of hnRNP A1.
PubMed
CAS
Google Scholar
Bonifaci N, Moroianu J, Radu A, Blobel G: Karyopherin beta2 mediates nuclear import of a mRNA binding protein. Proc Natl Acad Sci USA. 1997, 94: 5055-5060. 10.1073/pnas.94.10.5055. The authors cloned and sequenced the cDNA for human karyopherin β2 (transportin). Karyopherin β2/transportin binds directly to hnRNP A1 and is able to dock A1 at the pore as well as importing it into the nucleus.
Article
PubMed
CAS
PubMed Central
Google Scholar
Siomi MC, Eder PS, Kataoka N, Wan L, Liu Q, Dreyfuss G: Transportin-mediated nuclear import of heterogeneous nuclear RNP proteins. J Cell Biol. 1997, 138: 1181-1192. 10.1083/jcb.138.6.1181. Transportin 1 is shown to interact with, and mediate import of, hnRNPs. The authors also identify transportin 2, a transportin 1 homolog.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kataoka N, Bachorik JL, Dreyfuss G: Transportin-SR, a nuclear import receptor for SR proteins. J Cell Biol. 1999, 145: 1145-1152. 10.1083/jcb.145.6.1145. Describes a novel import receptor, transportin-SR, which binds directly to SR proteins, a group of abundant arginine/serine-rich proteins that include ASF/SF2 and SC35.
Article
PubMed
CAS
PubMed Central
Google Scholar
Lai MC, Lin RI, Huang SY, Tsai CW, Tarn WY: A human importin-beta family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J Biol Chem. 2000, 275: 7950-7957. 10.1074/jbc.275.11.7950. By using the human papillomavirus E2 activator, which contains an arginine/serine-rich domain, as a bait in a yeast two-hybrid screen the authors identified transportin-SR2, a new importin β family member.
Article
PubMed
CAS
Google Scholar
Pemberton LF, Rosenblum JS, Blobel G: Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting. J Cell Biol. 1999, 145: 1407-1417. 10.1083/jcb.145.7.1407. Kap114p was identified as the import receptor for TATA-binding protein. The authors show that the RanGTP-mediated dissociation of TATA-binding protein from Kap114p is stimulated by TATA-containing DNA and TFIIA.
Article
PubMed
CAS
PubMed Central
Google Scholar
Fornerod M, Ohno M, Yoshida M, Mattaj IW: CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997, 90: 1051-1060. Xenopus Crm1 binds cooperatively to an NES and RanGTP, and Crm1 mediates the nuclear export of NES-containing proteins.
Article
PubMed
CAS
Google Scholar
Ossareh-Nazari B, Bachelerie F, Dargemont C: Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science. 1997, 278: 141-144. 10.1126/science.278.5335.141. Interactions between human Crm1 and an NES-containing protein, were studied in reticulocyte lysates. An export assay using permeabilized cells was used to characterize the export of NES-containing proteins.
Article
PubMed
CAS
Google Scholar
Stade K, Ford CS, Guthrie C, Weis K: Exportin 1 (Crm1p) is an essential nuclear export factor. Cell. 1997, 90: 1041-1050. Identification of yeast Crm1p/Xpo1p as an NES export receptor using an in vivo export assay with a shuttling NES/NLS-green fluorescence protein reporter.
Article
PubMed
CAS
Google Scholar
Fukuda M, Asano S, Nakamura T, Adachi M, Yoshida M, Yanagida M, Nishida E: CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature. 1997, 390: 308-311. 10.1038/36894. The cytotoxin leptomycin Bis shown to be an inhibitor of NES-dependent nuclear export of proteins. In Xenopus oocyte extracts, a protein of 110 kDa that binds to the NES was found and characterized as Crm1.
Article
PubMed
CAS
Google Scholar
Sachdev S, Bagchi S, Zhang DD, Mings AC, Hannink M: Nuclear import of IkappaBalpha is accomplished by a ran-independent transport pathway. Mol Cell Biol. 2000, 20: 1571-1582. 10.1128/MCB.20.5.1571-1582.2000. The authors provide mechanistic insight into nuclear shuttling of IκBα. Nuclear import of IκBα occurs via a Ran-independent mechanism, while nuclear export was found to require the Ran-dependent Crm1 nuclear export receptor.
Article
PubMed
CAS
PubMed Central
Google Scholar
Paraskeva E, Izaurralde E, Bischoff FR, Huber J, Kutay U, Hartmann E, Luhrmann R, Görlich D: CRM1-mediated recycling of snurportin 1 to the cytoplasm. J Cell Biol. 1999, 145: 255-264. 10.1083/jcb.145.2.255. Re-export of snurportin 1 is mediated via Crm1. Snurportin 1 was found to be a potent competitor of other Crm1-dependent export pathways and is shown to bind to Crm1 with a high affinity.
Article
PubMed
CAS
PubMed Central
Google Scholar
Hakata Y, Umemoto T, Matsushita S, Shida H: Involvement of human CRM1 (exportin 1) in the export and multimerization of the Rex protein of human T-cell leukemia virus type 1. J Virol. 1998, 72: 6602-6607. The role of human exportin 1 in the export of Rex encoded by human T-cell leukemia virus type 1 is described.
PubMed
CAS
PubMed Central
Google Scholar
Ohno M, Segref A, Bachi A, Wilm M, Mattaj IW: PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation. Cell. 2000, 101: 187-198. U snRNA export requires an additional protein, named PHAX, which acts as an adaptor between the CBC-RNA complex and the CRM1-RanGTP proteins.
Article
PubMed
CAS
Google Scholar
Yang J, Bardes ES, Moore JD, Brennan J, Powers MA, Kornbluth S: Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev. 1998, 12: 2131-2143. The binding of Crm1 to the NES of cyclin B1 is demonstrated; phos-phorylation within the NES inhibits the interaction with Crm1. This suggests that cyclin B1 localization is controlled by phosphorylation.
Article
PubMed
CAS
PubMed Central
Google Scholar
Zhu J, McKeon F: NF-AT activation requires suppression of Crm1-dependent export by calcineurin. Nature. 1999, 398: 256-260. 10.1038/18473. The authors show that nuclear import of nuclear factor of activated T cells (NF-AT) is not sufficient to activate NF-AT target genes, and that NF-AT is exported to the cytoplasm using the Crm1 export pathway.
Article
PubMed
CAS
Google Scholar
Yan C, Lee LH, Davis LI: Crm1p mediates regulated nuclear export of a yeast AP-1-like transcription factor. EMBO J. 1998, 17: 7416-7429. 10.1093/emboj/17.24.7416. Characterization of Yap1p as a target of Crm1-mediated export. Recognition of Yap1p by Crm1p is inhibited by oxidation, and this inhibition requires cysteine residues flanking the NES.
Article
PubMed
CAS
PubMed Central
Google Scholar
Jensen TH, Neville M, Rain JC, McCarthy T, Legrain P, Rosbash M: Identification of novel Saccharomyces cerevisiae proteins with nuclear export activity: cell cycle-regulated transcription factor Ace2p shows cell cycle-independent nucleocytoplasmic shuttling. Mol Cell Biol. 2000, 20: 8047-8058. 10.1128/MCB.20.21.8047-8058.2000. The results of a yeast two-hybrid screen using S. cerevisiae Crm1p as a bait are described. New proteins with export activity (named Cip1p to Cip3p) were found. Cip3p is the cell-cycle-regulated transcription factor Ace2p, which contains both an NES and an NLS activity and enters the nucleus at all stages of the cell cycle.
Article
PubMed
CAS
PubMed Central
Google Scholar
Ferrigno P, Posas F, Koepp D, Saito H, Silver PA: Regulated nucleo/cytoplasmic exchange of HOG1 MAPK requires the importin beta homologs NMD5 and XPO1. EMBO J. 1998, 17: 5606-5614. 10.1093/emboj/17.19.5606. The localization of the osmotic stress-response MAP kinase Hog1p is controlled by Nmd5p and Crm1p. Hog1p phosphorylation triggers its nuclear import, whereas dephosphorylation is likely to promote its export via Crm1p.
Article
PubMed
CAS
PubMed Central
Google Scholar
Shulga N, James P, Craig EA, Goldfarb DS: A nuclear export signal prevents Saccharomyces cerevisiae Hsp70 Ssb1p from stimulating nuclear localization signal-directed nuclear transport. J Biol Chem. 1999, 274: 16501-16507. 10.1074/jbc.274.23.16501. Demonstrates a leucine-rich NES in the carboxy-terminal domain of Ssb1p and shows that it is responsible for both the different subcellular localizations of Ssa1p and Ssb1p and for their differential function in NLS-directed nuclear transport.
Article
PubMed
CAS
Google Scholar
Kutay U, Bischoff FR, Kostka S, Kraft R, Görlich D: Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell. 1997, 90: 1061-1071. CAS binds to importin α in a RanGTP-dependent manner and functions as an exportin for importin α.
Article
PubMed
CAS
Google Scholar
Hood JK, Silver PA: Cse1p is required for export of Srp1p/importin-alpha from the nucleus in Saccharomyces cerevisiae. J Biol Chem. 1998, 273: 35142-35146. 10.1074/jbc.273.52.35142. Cse1p is required for export of Srp1p (importin α) from the nucleus.
Article
PubMed
CAS
Google Scholar
Kunzler M, Hurt EC: Cse1p functions as the nuclear export receptor for importin alpha in yeast. FEBS Lett. 1998, 433: 185-190. 10.1016/S0014-5793(98)00892-8. Cse1p, Ran and importin a (Srp1p) interact in a yeast two-hybrid system and the recombinant proteins form a trimeric complex in vitro.
Article
PubMed
CAS
Google Scholar
Solsbacher J, Maurer P, Bischoff FR, Schlenstedt G: Cse1p is involved in export of yeast importin alpha from the nucleus. Mol Cell Biol. 1998, 18: 6805-6815. This paper characterizes the yeast homolog of CAS, which was previously identified as Cse1p. Cse1p forms a trimeric complex with Srp1p and RanGTP. Complex formation was prevented by NLS peptides, suggesting that importin α is exported only after cargo release.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kaffman A, Rank NM, O'Neill EM, Huang LS, O'Shea EK: The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus. Nature. 1998, 396: 482-486. 10.1038/24898. Nuclear export of the yeast transcription factor Pho4p is mediated by the exportin Msn5p. This is the first example of an NES regulated directly by phosphorylation.
Article
PubMed
CAS
Google Scholar
Yoshida K, Blobel G: The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins. J Cell Biol. 2001, 152: 729-739. 10.1083/jcb.152.4.729. Kap142p/Msn5p mediates nuclear export as well as nuclear import. The ssDNA-binding protein complex RPA was identified as an import cargo for Kap142p/Msn5p.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kutay U, Lipowsky G, Izaurralde E, Bischoff FR, Schwarzmaier P, Hartmann E, Görlich D: Identification of a tRNA-specific nuclear export receptor. Mol Cell. 1998, 1: 359-369. Together with [67], this paper characterizes the exportin that is involved in export of t-RNA. See annotation to [67].
Article
PubMed
CAS
Google Scholar
Arts GJ, Fornerod M, Mattaj IW: Identification of a nuclear export receptor for tRNA. Curr Biol. 1998, 8: 305-314. This paper identifies the function of exportin-t, which was previously identified as an uncharacterized member of the importin-β family. Exportin-t was found to stimulate the export of tRNA from microinjected Xenopus nuclei, to shuttle between the nucleus and cytoplasm and to bind tRNA in a RanGTP-dependent manner. Exportin-t is the first exportin to be shown to bind directly to a nucleic acid.
Article
PubMed
CAS
Google Scholar
Hellmuth K, Lau DM, Bischoff FR, Kunzler M, Hurt E, Simos G: Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport factor for tRNA. Mol Cell Biol. 1998, 18: 6374-6386. Los1p binds to nucleoporins and to RanGTP. Formation of the trimeric Los1p-Ran-GTP complex was stimulated in the presence of tRNA.
Article
PubMed
CAS
PubMed Central
Google Scholar
Weis K: Importins and exportins: how to get in and out of the nucleus. Trends Biochem Sci. 1998, 23: 185-189. 10.1016/S0968-0004(98)01204-3. A detailed review of nucleocytoplasmic transport and the individual transport pathways.
Article
PubMed
CAS
Google Scholar
Nachury MV, Weis K: The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci USA. 1999, 96: 9622-9627. 10.1073/pnas.96.17.9622. The directionality of nuclear transport is dependent on the compartmentalized distribution of RanGTP and that the direction of transport can be inverted in vitro by cytoplasmic addition of a GTP-bound mutant Ran, RanQ69LGTP.
Article
PubMed
CAS
PubMed Central
Google Scholar
Izaurralde E, Kutay U, von Kobbe C, Mattaj IW, Görlich D: The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 1997, 16: 6535-6547. 10.1093/emboj/16.21.6535. Using microinjection experiments, the authors demonstrate that the asymmetric distribution of RanGTP is crucial for many nucleocytoplasmic transport pathways.
Article
PubMed
CAS
PubMed Central
Google Scholar
Bischoff FR, Ponstingl H: Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature. 1991, 354: 80-82. 10.1038/354080a0. RCC1 is indentified as the guanine-nucleotide exchange factor of Ran.
Article
PubMed
CAS
Google Scholar
Bischoff FR, Klebe C, Kretschmer J, Wittinghofer A, Ponstingl H: RanGAP1 induces GTPase activity of nuclear Ras-related Ran. Proc Natl Acad Sci USA. 1994, 91: 2587-2591. The purification and identification of the Ran GTPase-activating protein, RanGAP1, a nuclear homodimeric 65 kDa protein.
Article
PubMed
CAS
PubMed Central
Google Scholar
Bischoff FR, Krebber H, Smirnova E, Dong W, Ponstingl H: Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 1995, 14: 705-715. The authors characterize RanBP1, which binds tightly to RanGTP. RanBP1 does not activate the RanGTPase alone, but cooperates with RanGAP1.
PubMed
CAS
PubMed Central
Google Scholar
Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E: Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J Biol Chem. 1995, 270: 14209-14213. 10.1074/jbc.270.23.14209. The authors report the characterization of a NPC-localized 358 kDa Ran-binding protein, Nup358 (RanBP2).
Article
PubMed
CAS
Google Scholar
Yokoyama N, Hayashi N, Seki N, Pante N, Ohba T, Nishii K, Kuma K, Hayashida T, Miyata T, Aebi U, et al: A giant nucleopore protein that binds Ran/TC4. Nature. 1995, 376: 184-188. 10.1038/376184a0. The identification and characterization of a 3224-residue nuclear pore protein, RanBP2 (Nup358), that interacts with RanGTP
Article
PubMed
CAS
Google Scholar
Ben-Efraima I, Gerace L: Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import. J Cell Biol. 2001, 152: 411-417. 10.1083/jcb.152.2.411. Using a solid-phase binding analysis, the affinity of an importin-β-cargo complex for different nucleoporins was determined. The results support a model in which importin β binds to nucleoporins with progressively increasing affinity as the import complex moves from the cytoplasmic to the central and the nucleoplasmic regions of the NPC.
Article
Google Scholar
Dostie J, Ferraiuolo M, Pause A, Adam SA, Sonenberg N: A novel shuttling protein, 4E-T, mediates the nuclear import of the mRNA 5' cap-binding protein, eIF4E. EMBO J. 2000, 19: 3142-3156. 10.1093/emboj/19.12.3142. The cloning and the characterization of an eIF4E-binding protein, 4E-T (eIF4E-transporter). 4E-T was found to be a nucleocytoplasmic shuttling protein that targets eIF4E for nuclear import.
Article
PubMed
CAS
PubMed Central
Google Scholar
Rosenblum JS, Pemberton LF, Blobel G: A nuclear import pathway for a protein involved in tRNA maturation. J Cell Biol. 1997, 139: 1655-1661. 10.1083/jcb.139.7.1655. Demonstrates that the yeast La protein Lhp1p is specifically imported by the importin-β-like protein Kap108p/Sxm1p.
Article
PubMed
CAS
PubMed Central
Google Scholar
Senger B, Simos G, Bischoff FR, Podtelejnikov A, Mann M, Hurt E: Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J. 1998, 17: 2196-2207. 10.1093/emboj/17.8.2196. MTR10 genetically interacts with NUP85 and is responsible for the nuclear import of Npl3p.
Article
PubMed
CAS
PubMed Central
Google Scholar
Albertini M, Pemberton LF, Rosenblum JS, Blobel G: A novel nuclear import pathway for the transcription factor TFIIS. J Cell Biol. 1998, 143: 1447-1455. 10.1083/jcb.143.6.1447. The yeast protein Nmd5p/Kap119p functions as an importin for the transcription elongation factor TFIIS.
Article
PubMed
CAS
PubMed Central
Google Scholar
Kaffman A, Rank NM, O'Shea EK: Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 1998, 12: 2673-2683. Pho4p is imported into the nucleus via Pse1p/Kap121p. The interaction between Pho4p and Pse1p is inhibited by phosphorylation, suggesting that phosphorylation of Pho4p regulates its import.
Article
PubMed
CAS
PubMed Central
Google Scholar
Chaves SR, Blobel G: Nuclear import of Spo12p, a protein essential for meiosis. J Biol Chem. 2001, 276: 17712-17717. 10.1074/jbc.M010760200. Demonstrates that Spo12p is imported into the nucleus by the karyopherin Kap121p/Pse1p.
Article
PubMed
CAS
Google Scholar
Titov AA, Blobel G: The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus. J Cell Biol. 1999, 147: 235-246. 10.1083/jcb.147.2.235. Characterization of Pdr6p/Kap122p. A complex of the large subunit (Toa1p) and the small subunit (Toa2p) of TFIIA was identified as an import substrate for Kap122p.
Article
PubMed
CAS
PubMed Central
Google Scholar
Lipowsky G, Bischoff FR, Schwarzmaier P, Kraft R, Kostka S, Hartmann E, Kutay U, Görlich D: Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes. EMBO J. 2000, 19: 4362-4371. 10.1093/emboj/19.16.4362. The identification of exportin 4 as an exportin for eIF-5A. The export signal in eIF-5A involves its unique hypusine modification.
Article
PubMed
CAS
PubMed Central
Google Scholar
DeVit MJ, Johnston M: The nuclear exportin Msn5p is required for nuclear export of the Mig1p glucose repressor of Saccharomyces cerevisiae. Curr Biol. 1999, 9: 1231-1241. 10.1016/S0960-9822(99)80503-X. Demonstrates that Msn5, a member of the importin β family, is required to mediate the regulated export of Mig1 from the nucleus.
Article
PubMed
CAS
Google Scholar
Blondel M, Alepuz PM, Huang LS, Shaham S, Ammerer G, Peter M: Nuclear export of Far1p in response to pheromones requires the export receptor Msn5p/Ste21p. Genes Dev. 1999, 13: 2284-2300. 10.1101/gad.13.17.2284. Far1p is exported in an Msn5p-dependent manner in response to pheromone treatment.
Article
PubMed
CAS
PubMed Central
Google Scholar
Mahanty SK, Wang Y, Farley FW, Elion EA: Nuclear shuttling of yeast scaffold Ste5 is required for its recruitment to the plasma membrane and activation of the mating MAPK cascade. Cell. 1999, 98: 501-512. The authors show that Ste5p is a shuttling protein whose nuclear export is stimulated by pheromone. Ste5p export seems to be dependent on MSN5.
Article
PubMed
CAS
Google Scholar
Görlich D, Dabrowski M, Bischoff FR, Kutay U, Bork P, Hartmann E, Prehn S, Izaurralde E: A novel class of RanGTP binding proteins. J Cell Biol. 1997, 138: 65-80. 10.1083/jcb.138.1.65. This paper describes the novel superfamily of Ran-binding proteins that includes importin β. Two proteins are characterized in more detail, namely RanBP7 and RanBP8. Both resemble importin β in their interaction with Ran, and both bind directly to nuclear pore complexes.
Article
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