Visualization of human karyopherin beta-1/importin beta-1 interactions with protein partners in mitotic cells by co-immunoprecipitation and proximity ligation assays [PDF]
Scientific Reports, 2018 AbstractKaryopherin beta-1/Importin beta-1 is a conserved nuclear transport receptor, acting in protein nuclear import in interphase and as a global regulator of mitosis. These pleiotropic functions reflect its ability to interact with, and regulate, different pathways during the cell cycle, operating as a major effector of the GTPase RAN.
Di Francesco Laura +7 more
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Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of β-catenin [PDF]
Current Biology, 1998 Control of the nuclear localization of specific proteins is an important mechanism for regulating many signal transduction pathways. Upon activation of the Wnt signaling pathway, beta-catenin localizes into the nucleus and interacts with TCF/LEF-1 (T-cell factor/lymphocyte enhancer factor-1) transcription factors, triggering activation of downstream ...
Fagotto, F. ; https://orcid.org/0000-0002-1495-2112 +2 more
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Expression in yeast of binding regions of karyopherins α and β inhibits nuclear import and cell growth [PDF]
Proceedings of the National Academy of Sciences, 1996 Using truncated forms of recombinant yeast karyopherins α and β in in vitro binding assays, we mapped the regions of karyopherin α that bind to karyopherin β and the regions of karyopherin β that interact with karyopherin α and with Ran-GTP.
C, Enenkel, N, Schülke, G, Blobel
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Rules for Nuclear Localization Sequence Recognition by Karyopherinβ2 [PDF]
Cell, 2006 Karyopherinbeta (Kapbeta) proteins bind nuclear localization and export signals (NLSs and NESs) to mediate nucleocytoplasmic trafficking, a process regulated by Ran GTPase through its nucleotide cycle. Diversity and complexity of signals recognized by Kap betas have prevented prediction of new Kap beta substrates.
Lee, Brittany J. +5 more
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Purification of Protein A-tagged Yeast Ran Reveals Association with a Novel Karyopherin β Family Member, Pdr6p [PDF]
Journal of Biological Chemistry, 2000 The small GTPase Ran (encoded by GSP1 and GSP2 in yeast) plays a central role in nucleocytoplasmic transport. GSP1 and GSP2 were tagged with protein A and functionally expressed in a gsp1 null mutant. After affinity purification of protein A-tagged Gsp1p or Gsp2p by IgG-Sepharose chromatography, known karyopherin beta transport receptors (e.g.
D, Lau +6 more
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The Nucleoporin Nup98 Is a Site for GDP/GTP Exchange on Ran and Termination of Karyopherin β2-mediated Nuclear Import [PDF]
Journal of Biological Chemistry, 2000 Karyopherin beta2 (Kapbeta2, transportin) binds the M9 sequence of human ribonucleoprotein A1 and mediates its nuclear import. Here we show a role for the nucleoporin Nup98 in the disassembly of Kapbeta2 import complexes at the nuclear side of the nuclear pore complex (NPC). Kapbeta2 bound to a region at the N terminus of Nup98 that contains an M9-like
B M, Fontoura, G, Blobel, N R, Yaseen
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Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta. [PDF]
Proceedings of the National Academy of Sciences, 1996 The alpha subunit of the karyopherin heterodimer functions in recognition of the protein import substrate and the beta subunit serves to dock the trimeric complex to one of many sites on nuclear pore complex fibers. The small GTPase Ran and the Ran interactive protein, p10, function in the release of the docked complex.
J, Moroianu, G, Blobel, A, Radu
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Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. [PDF]
Proceedings of the National Academy of Sciences, 1995 Although only 44% identical to human karyopherin alpha 1, human karyopherin alpha 2 (Rch1 protein) substituted for human karyopherin alpha 1 (hSRP-1/NPI-1) in recognizing a standard nuclear localization sequence and karyopherin beta-dependent targeting to the nuclear envelope of digitonin-permeabilized cells.
J, Moroianu +3 more
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The Nuclear Transport Factor Karyopherin β Binds Stoichiometrically to Ran-GTP and Inhibits the Ran GTPase Activating Protein [PDF]
Journal of Biological Chemistry, 1996 The heterodimeric karyopherin functions in targeting a nuclear localization sequence (NLS)-containing protein to the nuclear pore complex followed by Ran-GTP and p10-mediated translocation of the NLS protein into the nucleoplasm. It was shown recently that Ran-GTP dissociated the karyopherin heterodimer and, in doing so, associated with karyopherin ...
M, Floer, G, Blobel
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Ran Binding Domains Promote the Interaction of Ran with p97/β-Karyopherin, Linking the Docking and Translocation Steps of Nuclear Import [PDF]
Journal of Biological Chemistry, 1996 Nuclear protein import is accomplished by two sequential events; docking at the nuclear pore complex followed by ATP-dependent translocation across the nuclear envelope. Docking of nuclear targeted proteins requires a 56-kDa nuclear localization signal receptor (alpha-karyopherin, importin-alpha, SRP1 alpha) and a 97-kDa protein (beta-karyopherin ...
K M, Lounsbury +3 more
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