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Journal articles on the topic 'RanGAP'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Hutten, Saskia, Annette Flotho, Frauke Melchior та Ralph H. Kehlenbach. "The Nup358-RanGAP Complex Is Required for Efficient Importin α/β-dependent Nuclear Import". Molecular Biology of the Cell 19, № 5 (2008): 2300–2310. http://dx.doi.org/10.1091/mbc.e07-12-1279.

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In vertebrate cells, the nucleoporin Nup358/RanBP2 is a major component of the filaments that emanate from the nuclear pore complex into the cytoplasm. Nup358 forms a complex with SUMOylated RanGAP1, the GTPase activating protein for Ran. RanGAP1 plays a pivotal role in the establishment of a RanGTP gradient across the nuclear envelope and, hence, in the majority of nucleocytoplasmic transport pathways. Here, we investigate the roles of the Nup358-RanGAP1 complex and of soluble RanGAP1 in nuclear protein transport, combining in vivo and in vitro approaches. Depletion of Nup358 by RNA interfere

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2

HABERLAND, Jörg, and Volker GERKE. "Conserved charged residues in the leucine-rich repeat domain of the Ran GTPase activating protein are required for Ran binding and GTPase activation." Biochemical Journal 343, no. 3 (1999): 653–62. http://dx.doi.org/10.1042/bj3430653.

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GTPase activating proteins (GAPs) for Ran, a Ras-related GTPase participating in nucleocytoplasmic transport, have been identified in different species ranging from yeast to man. All RanGAPs are characterized by a conserved domain consisting of eight leucine-rich repeats (LRRs) interrupted at two positions by so-called separating regions, the latter being unique for RanGAPs within the family of LRR proteins. The cytosolic RanGAP activity is essential for the Ran GTPase cycle which in turn provides directionality in nucleocytoplasmic transport, but the structural basis for the interaction betwe

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3

Nishijima, Hitoshi, Jun-ichi Nakayama, Tomoko Yoshioka, et al. "Nuclear RanGAP Is Required for the Heterochromatin Assembly and Is Reciprocally Regulated by Histone H3 and Clr4 Histone Methyltransferase in Schizosaccharomyces pombe." Molecular Biology of the Cell 17, no. 6 (2006): 2524–36. http://dx.doi.org/10.1091/mbc.e05-09-0893.

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Although the Ran GTPase-activating protein RanGAP mainly functions in the cytoplasm, several lines of evidence indicate a nuclear function of RanGAP. We found that Schizosaccharomyces pombe RanGAP, SpRna1, bound the core of histone H3 (H3) and enhanced Clr4-mediated H3-lysine 9 (K9) methylation. This enhancement was not observed for methylation of the H3-tail containing K9 and was independent of SpRna1–RanGAP activity, suggesting that SpRna1 itself enhances Clr4-mediated H3-K9 methylation via H3. Although most SpRna1 is in the cytoplasm, some cofractionated with H3. Sprna1ts mutations caused d

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4

Seewald, Michael J., Astrid Kraemer, Marian Farkasovsky, Carolin Körner, Alfred Wittinghofer, and Ingrid R. Vetter. "Biochemical Characterization of the Ran-RanBP1-RanGAP System: Are RanBP Proteins and the Acidic Tail of RanGAP Required for the Ran-RanGAP GTPase Reaction?" Molecular and Cellular Biology 23, no. 22 (2003): 8124–36. http://dx.doi.org/10.1128/mcb.23.22.8124-8136.2003.

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ABSTRACT RanBP type proteins have been reported to increase the catalytic efficiency of the RanGAP-mediated GTPase reaction on Ran. Since the structure of the Ran-RanBP1-RanGAP complex showed RanBP1 to be located away from the active site, we reinvestigated the reaction using fluorescence spectroscopy under pre-steady-state conditions. We can show that RanBP1 indeed does not influence the rate-limiting step of the reaction, which is the cleavage of GTP and/or the release of product Pi. It does, however, influence the dynamics of the Ran-RanGAP interaction, its most dramatic effect being the 20

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5

Faustino, Randolph S., Delphine C. Rousseau, Melanie N. Landry, Annette L. Kostenuk, and Grant N. Pierce. "Effects of mitogen-activated protein kinases on nuclear protein importThis paper is one of a selection of papers published in this Special Issue, entitled The Nucleus: A Cell Within A Cell." Canadian Journal of Physiology and Pharmacology 84, no. 3-4 (2006): 469–75. http://dx.doi.org/10.1139/y05-131.

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ERK-2 MAP kinase activation induces inhibitory effects on nuclear protein import in vascular smooth muscle cells. The mechanism and characteristics of this effect of ERK-2 were investigated. An unusual dose-dependent effect of ERK-2 on nuclear protein import was identified. At higher concentrations (1 μg/mL) of ERK-2, nuclear protein import was stimulated, whereas lower concentrations (0.04 μg/mL) inhibited import. Intermediate concentrations exerted intermediate effects. The stimulatory and inhibitory effects at the 2 different ERK-2 concentrations were observed in both conventional, permeabi

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6

Askjaer, Peter, Angela Bachi, Matthias Wilm, et al. "RanGTP-Regulated Interactions of CRM1 with Nucleoporins and a Shuttling DEAD-Box Helicase." Molecular and Cellular Biology 19, no. 9 (1999): 6276–85. http://dx.doi.org/10.1128/mcb.19.9.6276.

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ABSTRACT CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP. Using a quantitative CRM1-NES cargo binding assay, significant differences in affinity for CRM1 among natural NESs are demonstrated, suggesting that the steady-state nucleocytoplasmic distribution of shuttling proteins could be determined by the relative strengths of their NESs. We also show that a trimeric CRM1-NES-RanGTP complex is disassembled

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7

Meier, Iris, Xiao Zhou, Jelena Brkljacić, Annkatrin Rose, Qiao Zhao, and Xianfeng Morgan Xu. "Targeting proteins to the plant nuclear envelope." Biochemical Society Transactions 38, no. 3 (2010): 733–40. http://dx.doi.org/10.1042/bst0380733.

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The nuclear envelope and the nuclear pore are important structures that both separate and selectively connect the nucleoplasm and the cytoplasm. The requirements for specific targeting of proteins to the plant nuclear envelope and nuclear pore are poorly understood. How are transmembrane-domain proteins sorted to the nuclear envelope and nuclear pore membranes? What protein–protein interactions are involved in associating other proteins to the nuclear pore? Are there plant-specific aspects to these processes? We are using the case of the nuclear pore-associated Ran-cycle component RanGAP (Ran

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8

Gingell, Luke F., and Janna R. McLean. "A Protamine Knockdown Mimics the Function of Sd in Drosophila melanogaster." G3: Genes|Genomes|Genetics 10, no. 6 (2020): 2111–15. http://dx.doi.org/10.1534/g3.120.401307.

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Segregation Distorter (SD) is an autosomal meiotic drive system found worldwide in natural populations of Drosophila melanogaster. This gene complex induces the preferential and nearly exclusive transmission of the SD chromosome in SD/SD+ males. This selfish propagation occurs through the interplay of the Sd locus, its enhancers and the Rsps locus during spermatid development. The key distorter locus, Sd, encodes a truncated but enzymatically active RanGAP (RanGTPase-activating protein), a key nuclear transport factor in the Ran signaling pathway. When encoded by Sd, RanGAP is mislocalized to

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9

Seewald, Michael J., Carolin Körner, Alfred Wittinghofer, and Ingrid R. Vetter. "RanGAP mediates GTP hydrolysis without an arginine finger." Nature 415, no. 6872 (2002): 662–66. http://dx.doi.org/10.1038/415662a.

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10

Kusano, A., C. Staber, and B. Ganetzky. "Segregation distortion induced by wild-type RanGAP in Drosophila." Proceedings of the National Academy of Sciences 99, no. 10 (2002): 6866–70. http://dx.doi.org/10.1073/pnas.102165099.

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11

Kusano, Ayumi, Tomoko Yoshioka, Hitoshi Nishijima, Hideo Nishitani, and Takeharu Nishimoto. "Schizosaccharomyces pombe RanGAP Homolog, SpRna1, Is Required for Centromeric Silencing and Chromosome Segregation." Molecular Biology of the Cell 15, no. 11 (2004): 4960–70. http://dx.doi.org/10.1091/mbc.e04-01-0067.

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We isolated 11 independent temperature-sensitive (ts) mutants of Schizosaccharomyces pombe RanGAP, SpRna1 that have several amino acid changes in the conserved domains of RanGAP. Resulting Sprna1ts showed a strong defect in mitotic chromosome segregation, but did not in nucleocytoplasmic transport and microtubule formation. In addition to Sprna1+ and Spksp1+, the clr4+ (histone H3-K9 methyltransferase), the S. pombe gene, SPAC25A8.01c, designated snf2SR+ (a member of the chromatin remodeling factors, Snf2 family with DNA-dependent ATPase activity), but not the spi1+ (S. pombe Ran homolog), res

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12

Hinkle, Beth, Melissa M. Rolls, Pascal Stein, Tom Rapoport, and Mark Terasaki. "Ran is associated with chromosomes during starfish oocyte meiosis and embryonic mitoses." Zygote 8, S1 (1999): S91. http://dx.doi.org/10.1017/s0967199400130540.

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Ran is an abundant small G protein that has a central role in nuclear transport during interphase. Ran function depends on distinct pools of RanGTP in the nucleus and RanGDP in the cytoplasm, which are maintained by compartmentalisation of the nucleotide exchange and GTPase activating proteins for Ran. RCC1 (Regulator of Chromosome Condensation) is the only known guanine nucleotide exchange factor for Ran and is associated with chromatin. RanGAPl together with RanBPl are the primary GTPase activator proteins and are located in the cytoplasm.Ran function in nuclear transport is clearly inactiva

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13

Merrill, C. "Truncated RanGAP Encoded by the Segregation Distorter Locus of Drosophila." Science 283, no. 5408 (1999): 1742–45. http://dx.doi.org/10.1126/science.283.5408.1742.

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14

Feng, W., A. L. Benko, J. H. Lee, D. R. Stanford, and A. K. Hopper. "Antagonistic effects of NES and NLS motifs determine S. cerevisiae Rna1p subcellular distribution." Journal of Cell Science 112, no. 3 (1999): 339–47. http://dx.doi.org/10.1242/jcs.112.3.339.

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Nucleus/cytosol exchange requires a GTPase, Ran. In yeast Rna1p is the GTPase activating protein for Ran (RanGAP) and Prp20p is the Ran GDP/GTP exchange factor (GEF). RanGAP is primarily cytosolic and GEF is nuclear. Their subcellular distributions led to the prediction that Ran-GTP hydrolysis takes place solely in the cytosol and GDP/GTP exchange solely in the nucleus. Current models propose that the Ran-GTP/Ran-GDP gradient across the nuclear membrane determines the direction of exchange. We provide three lines of evidence that Rna1p enters and leaves the nuclear interior. (1) Rna1p possesse

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15

Askjaer, Peter, Vincent Galy, Eva Hannak та Iain W. Mattaj. "Ran GTPase Cycle and Importins α and β Are Essential for Spindle Formation and Nuclear Envelope Assembly in LivingCaenorhabditis elegans Embryos". Molecular Biology of the Cell 13, № 12 (2002): 4355–70. http://dx.doi.org/10.1091/mbc.e02-06-0346.

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The small GTPase Ran has been found to play pivotal roles in several aspects of cell function. We have investigated the role of the Ran GTPase cycle in spindle formation and nuclear envelope assembly in dividing Caenorhabditis elegans embryos in real time. We found that Ran and its cofactors RanBP2, RanGAP, and RCC1 are all essential for reformation of the nuclear envelope after cell division. Reducing the expression of any of these components of the Ran GTPase cycle by RNAi leads to strong extranuclear clustering of integral nuclear envelope proteins and nucleoporins. Ran, RanBP2, and RanGAP

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16

Kusano, Ayumi, Cynthia Staber, and Barry Ganetzky. "Nuclear Mislocalization of Enzymatically Active RanGAP Causes Segregation Distortion in Drosophila." Developmental Cell 1, no. 3 (2001): 351–61. http://dx.doi.org/10.1016/s1534-5807(01)00042-9.

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17

Jeong, Sun Yong, Annkatrin Rose, Jomon Joseph, Mary Dasso, and Iris Meier. "Plant-specific mitotic targeting of RanGAP requires a functional WPP domain." Plant Journal 42, no. 2 (2005): 270–82. http://dx.doi.org/10.1111/j.1365-313x.2005.02368.x.

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18

Fujiwara, Kazushiro, Koichi Hasegawa, Masahiro Oka, Yoshihiro Yoneda, and Kazuaki Yoshikawa. "Terminal differentiation of cortical neurons rapidly remodels RanGAP-mediated nuclear transport system." Genes to Cells 21, no. 11 (2016): 1176–94. http://dx.doi.org/10.1111/gtc.12434.

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19

Rodrigo-Peiris, Thushani, Xianfeng Morgan Xu, Qiao Zhao, Horng-Jing Wang, and Iris Meier. "RanGAP is required for post-meiotic mitosis in female gametophyte development in Arabidopsis thaliana." Journal of Experimental Botany 62, no. 8 (2011): 2705–14. http://dx.doi.org/10.1093/jxb/erq448.

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20

Zhou, Xiao, Katja Graumann, David E. Evans, and Iris Meier. "Novel plant SUN–KASH bridges are involved in RanGAP anchoring and nuclear shape determination." Journal of Cell Biology 196, no. 2 (2012): 203–11. http://dx.doi.org/10.1083/jcb.201108098.

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Inner nuclear membrane Sad1/UNC-84 (SUN) proteins interact with outer nuclear membrane (ONM) Klarsicht/ANC-1/Syne homology (KASH) proteins, forming linkers of nucleoskeleton to cytoskeleton conserved from yeast to human and involved in positioning of nuclei and chromosomes. Defects in SUN–KASH bridges are linked to muscular dystrophy, progeria, and cancer. SUN proteins were recently identified in plants, but their ONM KASH partners are unknown. Arabidopsis WPP domain–interacting proteins (AtWIPs) are plant-specific ONM proteins that redundantly anchor Arabidopsis RanGTPase–activating protein 1

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21

Xu, Xianfeng Morgan, Tea Meulia, and Iris Meier. "Anchorage of Plant RanGAP to the Nuclear Envelope Involves Novel Nuclear-Pore-Associated Proteins." Current Biology 17, no. 13 (2007): 1157–63. http://dx.doi.org/10.1016/j.cub.2007.05.076.

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22

Faustino, Randolph S., Lyle N. W. Stronger, Melanie N. Richard, et al. "RanGAP-Mediated Nuclear Protein Import in Vascular Smooth Muscle Cells Is Augmented by Lysophosphatidylcholine." Molecular Pharmacology 71, no. 2 (2006): 438–45. http://dx.doi.org/10.1124/mol.105.021667.

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23

Torosantucci, Liliana, Maria De Luca, Giulia Guarguaglini, Patrizia Lavia, and Francesca Degrassi. "Localized RanGTP Accumulation Promotes Microtubule Nucleation at Kinetochores in Somatic Mammalian Cells." Molecular Biology of the Cell 19, no. 5 (2008): 1873–82. http://dx.doi.org/10.1091/mbc.e07-10-1050.

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Centrosomes are the major sites for microtubule nucleation in mammalian cells, although both chromatin- and kinetochore-mediated microtubule nucleation have been observed during spindle assembly. As yet, it is still unclear whether these pathways are coregulated, and the molecular requirements for microtubule nucleation at kinetochore are not fully understood. This work demonstrates that kinetochores are initial sites for microtubule nucleation during spindle reassembly after nocodazole. This process requires local RanGTP accumulation concomitant with delocalization from kinetochores of the hy

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24

Shen, Xu, Hua Zeng, Liang Xie, et al. "The GTPase Activating Rap/RanGAP Domain-Like 1 Gene Is Associated with Chicken Reproductive Traits." PLoS ONE 7, no. 4 (2012): e33851. http://dx.doi.org/10.1371/journal.pone.0033851.

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25

Boruc, Joanna, Anna H. N. Griffis, Thushani Rodrigo-Peiris, et al. "GAP Activity, but Not Subcellular Targeting, Is Required for Arabidopsis RanGAP Cellular and Developmental Functions." Plant Cell 27, no. 7 (2015): 1985–98. http://dx.doi.org/10.1105/tpc.114.135780.

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26

Rose, A., and I. Meier. "A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim." Proceedings of the National Academy of Sciences 98, no. 26 (2001): 15377–82. http://dx.doi.org/10.1073/pnas.261459698.

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27

Khrenova, Maria G., Bella L. Grigorenko, and Alexander V. Nemukhin. "Molecular Modeling Reveals the Mechanism of Ran-RanGAP-Catalyzed Guanosine Triphosphate Hydrolysis without an Arginine Finger." ACS Catalysis 11, no. 15 (2021): 8985–98. http://dx.doi.org/10.1021/acscatal.1c00582.

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28

Yabuuchi, Takatoshi, Tomonori Nakai, Seiji Sonobe, Daisuke Yamauchi, and Yoshinobu Mineyuki. "Preprophase band formation and cortical division zone establishment: RanGAP behaves differently from microtubules during their band formation." Plant Signaling & Behavior 10, no. 9 (2015): e1060385. http://dx.doi.org/10.1080/15592324.2015.1060385.

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29

Bibak, Niloufar, Rachelle M. J. Paul, Douglas M. Freymann, and Nabeel R. Yaseen. "Purification of RanGDP, RanGTP, and RanGMPPNP by ion exchange chromatography." Analytical Biochemistry 333, no. 1 (2004): 57–64. http://dx.doi.org/10.1016/j.ab.2004.06.017.

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30

de Boor, Susanne, Philipp Knyphausen, Nora Kuhlmann, et al. "Small GTP-binding protein Ran is regulated by posttranslational lysine acetylation." Proceedings of the National Academy of Sciences 112, no. 28 (2015): E3679—E3688. http://dx.doi.org/10.1073/pnas.1505995112.

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Ran is a small GTP-binding protein of the Ras superfamily regulating fundamental cellular processes: nucleo-cytoplasmic transport, nuclear envelope formation and mitotic spindle assembly. An intracellular Ran•GTP/Ran•GDP gradient created by the distinct subcellular localization of its regulators RCC1 and RanGAP mediates many of its cellular effects. Recent proteomic screens identified five Ran lysine acetylation sites in human and eleven sites in mouse/rat tissues. Some of these sites are located in functionally highly important regions such as switch I and switch II. Here, we show that lysine

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31

Haberland, Jörg, Jörg Becker, and Volker Gerke. "The Acidic C-terminal Domain of rna1p Is Required for the Binding of Ran·GTP and for RanGAP Activity." Journal of Biological Chemistry 272, no. 39 (1997): 24717–26. http://dx.doi.org/10.1074/jbc.272.39.24717.

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32

Sacco, Melanie A., Shahid Mansoor, and Peter Moffett. "A RanGAP protein physically interacts with the NB-LRR protein Rx, and is required for Rx-mediated viral resistance." Plant Journal 52, no. 1 (2007): 82–93. http://dx.doi.org/10.1111/j.1365-313x.2007.03213.x.

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33

Ohba, Tomoyuki, Hitoshi Nishijima, Hideo Nishitani, and Takeharu Nishimoto. "Schizosaccharomyces pombe Snf2SR, a novel SNF2 family protein, interacts with Ran GTPase and modulates both RanGEF and RanGAP activities." Genes to Cells 13, no. 6 (2008): 571–82. http://dx.doi.org/10.1111/j.1365-2443.2008.01190.x.

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34

Görlich, D., N. Panté, U. Kutay, U. Aebi, and F. R. Bischoff. "Identification of different roles for RanGDP and RanGTP in nuclear protein import." EMBO Journal 15, no. 20 (1996): 5584–94. http://dx.doi.org/10.1002/j.1460-2075.1996.tb00943.x.

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35

Yabuuchi, Takatoshi, Tomonori Nakai, Daisuke Yamauchi, Seiji Sonobe, and Yoshinobu Mineyuki. "C3-P-15Spatio-temporal differences between RanGAP and microtubule bands during the development of preprophase bands in onion root tip cells." Microscopy 64, suppl 1 (2015): i133.2—i133. http://dx.doi.org/10.1093/jmicro/dfv318.

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36

Sarkar, Srimonti, and Anita K. Hopper. "tRNA Nuclear Export in Saccharomyces cerevisiae: In Situ Hybridization Analysis." Molecular Biology of the Cell 9, no. 11 (1998): 3041–55. http://dx.doi.org/10.1091/mbc.9.11.3041.

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To understand the factors specifically affecting tRNA nuclear export, we adapted in situ hybridization procedures to locate endogenous levels of individual tRNA families in wild-type and mutant yeast cells. Our studies of tRNAs encoded by genes lacking introns show that nucleoporin Nup116p affects both poly(A) RNA and tRNA export, whereas Nup159p affects only poly(A) RNA export. Los1p is similar to exportin-t, which facilitates vertebrate tRNA export. Alos1 deletion mutation affects tRNA but not poly(A) RNA export. The data support the notion that Los1p and exportin-t are functional homologues

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37

Goffin, Laurence, Sadanand Vodala, Christine Fraser та ін. "The Unfolded Protein Response Transducer Ire1p Contains a Nuclear Localization Sequence Recognized by Multiple β Importins". Molecular Biology of the Cell 17, № 12 (2006): 5309–23. http://dx.doi.org/10.1091/mbc.e06-04-0292.

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The Ire1p transmembrane receptor kinase/endonuclease transduces the unfolded protein response (UPR) from the endoplasmic reticulum (ER) to the nucleus in Saccharomyces cerevisiae. In this study, we analyzed the capacity of a highly basic sequence in the linker region of Ire1p to function as a nuclear localization sequence (NLS) both in vivo and in vitro. This 18-residue sequence is capable of targeting green fluorescent protein to the nucleus of yeast cells in a process requiring proteins involved in the Ran GTPase cycle that facilitates nuclear import. Mutagenic analysis and importin binding

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38

Görlich, Dirk, Marylena Dabrowski, F. Ralf Bischoff, et al. "A Novel Class of RanGTP Binding Proteins." Journal of Cell Biology 138, no. 1 (1997): 65–80. http://dx.doi.org/10.1083/jcb.138.1.65.

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The importin-α/β complex and the GTPase Ran mediate nuclear import of proteins with a classical nuclear localization signal. Although Ran has been implicated also in a variety of other processes, such as cell cycle progression, a direct function of Ran has so far only been demonstrated for importin-mediated nuclear import. We have now identified an entire class of ∼20 potential Ran targets that share a sequence motif related to the Ran-binding site of importin-β. We have confirmed specific RanGTP binding for some of them, namely for two novel factors, RanBP7 and RanBP8, for CAS, Pse1p, and Msn

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39

Deane, R., W. Schäfer, H. P. Zimmermann, et al. "Ran-binding protein 5 (RanBP5) is related to the nuclear transport factor importin-beta but interacts differently with RanBP1." Molecular and Cellular Biology 17, no. 9 (1997): 5087–96. http://dx.doi.org/10.1128/mcb.17.9.5087.

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We report the identification and characterization of a novel 124-kDa Ran binding protein, RanBP5. This protein is related to importin-beta, the key mediator of nuclear localization signal (NLS)-dependent nuclear transport. RanBP5 was identified by two independent methods: it was isolated from HeLa cells by using its interaction with RanGTP in an overlay assay to monitor enrichment, and it was also found by the yeast two-hybrid selection method with RanBP1 as bait. RanBP5 binds to RanBP1 as part of a trimeric RanBP1-Ran-RanBP5 complex. Like importin-beta, RanBP5 strongly binds the GTP-bound for

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40

Zhao, Qiao, Jelena Brkljacic, and Iris Meier. "Two Distinct Interacting Classes of Nuclear Envelope–Associated Coiled-Coil Proteins Are Required for the Tissue-Specific Nuclear Envelope Targeting of Arabidopsis RanGAP." Plant Cell 20, no. 6 (2008): 1639–51. http://dx.doi.org/10.1105/tpc.108.059220.

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41

Meier, I., Q. Zhao, J. Brkljacic, and X. Morgan Xu. "Two distinct, interacting classes of nuclear envelope-associated coiled-coil proteins are required for the tissue-specific nuclear envelope targeting of Arabidopsis RanGAP." Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology 150, no. 3 (2008): S199. http://dx.doi.org/10.1016/j.cbpa.2008.04.550.

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42

Stewart, M. "Structural basis for the nuclear protein import cycle." Biochemical Society Transactions 34, no. 5 (2006): 701–4. http://dx.doi.org/10.1042/bst0340701.

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Transport of macromolecules between the nuclear and cytoplasmic compartments through NPCs (nuclear pore complexes) is mediated by soluble transport factors that are commonly members of the importin-β superfamily. In the nuclear protein import cycle, importin-β binds cargo in the cytoplasm (usually via the importin-α adaptor) and transports it through NPCs with which it interacts transiently by way of NPC proteins (‘nucleoporins’) that contain distinctive FG (Phe-Gly) sequence repeats. In the nucleus, Ran-GTP binds to importin-β, dissociating the import complex. The importin-β–Ran-GTP complex r

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43

Timinszky, Gyula, László Tirián, Ferenc T. Nagy та ін. "The importin-β P446L dominant-negative mutant protein loses RanGTP binding ability and blocks the formation of intact nuclear envelope". Journal of Cell Science 115, № 8 (2002): 1675–87. http://dx.doi.org/10.1242/jcs.115.8.1675.

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Three of the four independently induced KetelDdominantnegative female sterile mutations that identify the Drosophila importin-β gene, originated from a C4114→ T transition and the concurrent replacement of Pro446 by Leu (P446L). CD spectroscopy of representative peptides with Pro or Leu in the crucial position revealed that upon the Pro→Leu exchange the P446L mutant protein loses flexibility and attains most likely an open conformation. The P446L mutation abolishes RanGTP binding of the P446L mutant form of importin-β protein and results in increased RanGDP binding ability. Notably, the P446L

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44

Lounsbury, Karen M., та Ian G. Macara. "Ran-binding Protein 1 (RanBP1) Forms a Ternary Complex with Ran and Karyopherin β and Reduces Ran GTPase-activating Protein (RanGAP) Inhibition by Karyopherin β". Journal of Biological Chemistry 272, № 1 (1997): 551–55. http://dx.doi.org/10.1074/jbc.272.1.551.

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Chafe, Shawn C., and Dev Mangroo. "Scyl1 Facilitates Nuclear tRNA Export in Mammalian Cells by Acting at the Nuclear Pore Complex." Molecular Biology of the Cell 21, no. 14 (2010): 2483–99. http://dx.doi.org/10.1091/mbc.e10-03-0176.

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Scyl1 is an evolutionarily conserved N-terminal protein kinase-like domain protein that plays a role in COP1-mediated retrograde protein trafficking in mammalian cells. Furthermore, loss of Scyl1 function has been shown to result in neurodegenerative disorders in mice. Here, we report that Scyl1 is also a cytoplasmic component of the mammalian nuclear tRNA export machinery. Like exportin-t, overexpression of Scyl1 restored export of a nuclear export-defective serine amber suppressor tRNA mutant in COS-7 cells. Scyl1 binds tRNA saturably, and associates with the nuclear pore complex by interact

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Greenberg Temin, Rayla. "Analysis of a Strong Suppressor of Segregation Distorter in Drosophila melanogaster." Genetics 215, no. 4 (2020): 1085–105. http://dx.doi.org/10.1534/genetics.120.303150.

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Segregation Distorter (SD) is a naturally occurring male meiotic drive system in Drosophila melanogaster, characterized by almost exclusive transmission of the SD chromosome owing to dysfunction of sperm receiving the SD+ homolog. Previous studies identified at least three closely linked loci on chromosome 2 required for distortion: Sd, the primary distorting gene; E(SD) (Enhancer of SD), which increases the strength of distortion; and Rsp (Responder), the apparent target of Sd. Strength of distortion is also influenced by linked upward modifiers including M(SD) (Modifier of SD) and St(SD) (St

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Albertini, Markus, Lucy F. Pemberton, Jonathan S. Rosenblum, and Günter Blobel. "A Novel Nuclear Import Pathway for the Transcription Factor TFIIS." Journal of Cell Biology 143, no. 6 (1998): 1447–55. http://dx.doi.org/10.1083/jcb.143.6.1447.

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We have identified a novel pathway for protein import into the nucleus. We have shown that the previously identified but uncharacterized yeast protein Nmd5p functions as a karyopherin. It was therefore designated Kap119p (karyopherin with Mr of 119 kD). We localized Kap119p to both the nucleus and the cytoplasm. We identified the transcription elongation factor TFIIS as its major cognate import substrate. The cytoplasmic Kap119p exists as an approximately stoichiometric complex with TFIIS. RanGTP, not RanGDP, dissociated the isolated Kap119p/TFIIS complex and bound to Kap119p. Kap119p also bou

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Johnstone, Aaron D., Robert T. Mullen, and Dev Mangroo. "Arabidopsis At2g40730 encodes a cytoplasmic protein involved in nuclear tRNA export." Botany 89, no. 3 (2011): 175–90. http://dx.doi.org/10.1139/b10-090.

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Nuclear tRNA export plays an essential role in several key cellular processes, such as regulation of protein synthesis, cell cycle progression, response to nutrient availability and DNA damage, and development. While the overall mechanism of nuclear tRNA export is, in general, poorly understood, the details of specific steps are emerging from studies conducted in different organisms aimed at identifying and characterizing components involved in the process. Here, we report that Arabidopsis thaliana (L.) Heynh At2g40730 encodes CTEXP, a cytoplasmic protein component of the nuclear tRNA export p

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Guillem, Flavia, Michael Dussiot, Sebastien Causse, et al. "XPO1 (Exportin-1) Is a Major Regulator of Human Erythroid Differentiation. Potential Clinical Applications to Decrease Ineffective Erythropoiesis of Beta-Thalassemia." Blood 126, no. 23 (2015): 2368. http://dx.doi.org/10.1182/blood.v126.23.2368.2368.

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Abstract Background We and others have shown that normal human erythroid cell maturation requires a transient activation of caspase-3 at late stages of maturation (Zermati et al, J Exp Med 2001). We further documented that, in human erythroblasts, the chaperone HSP70 is constitutively expressed and, at late stages of maturation, translocates into the nucleus and protects GATA-1, the master transcriptional factor critical for erythropoiesis, from caspase-3 cleavage (Ribeil et al, Nature 2007). During the maturation of human β-TM erythroblasts, HSP70 is sequestrated by excess of α-globin chains

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Joseph, Jomon, Shyh-Han Tan, Tatiana S. Karpova, James G. McNally, and Mary Dasso. "SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles." Journal of Cell Biology 156, no. 4 (2002): 595–602. http://dx.doi.org/10.1083/jcb.200110109.

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RanGAP1 was the first documented substrate for conjugation with the ubiquitin-like protein SUMO-1. However, the functional significance of this conjugation has not been fully clarified. We sought to examine RanGAP1 behavior during mitosis. We found that RanGAP1 associates with mitotic spindles and that it is particularly concentrated at foci near kinetochores. Association with kinetochores appeared soon after nuclear envelope breakdown and persisted until late anaphase, but it was lost coincident with nuclear envelope assembly in telophase. A mutant RanGAP1 protein lacking the capacity to be c

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