User menu

Leukemia-Associated Mutations in Nucleophosmin Alter Recognition by CRM1: Molecular Basis of Aberrant Transport

Bibliographic reference Arregi, Igor ; Falces Ramos, Jorge ; Olazabal-Herrero, Anne ; Alonso-Mariño, Marián ; Taneva, Stefka G. ; et. al. Leukemia-Associated Mutations in Nucleophosmin Alter Recognition by CRM1: Molecular Basis of Aberrant Transport. In: PLoS One, Vol. 10, no.6, p. e0130610 (2015)
Permanent URL http://hdl.handle.net/2078.1/186279
  1. Lindström Mikael S., NPM1/B23: A Multifunctional Chaperone in Ribosome Biogenesis and Chromatin Remodeling, 10.1155/2011/195209
  2. Maggi L. B., Kuchenruether M., Dadey D. Y. A., Schwope R. M., Grisendi S., Townsend R. R., Pandolfi P. P., Weber J. D., Nucleophosmin Serves as a Rate-Limiting Nuclear Export Chaperone for the Mammalian Ribosome, 10.1128/mcb.01548-07
  3. Wang Wei, Budhu Anuradha, Forgues Marshonna, Wang Xin Wei, Temporal and spatial control of nucleophosmin by the Ran–Crm1 complex in centrosome duplication, 10.1038/ncb1282
  4. Colombo Emanuela, Marine Jean-Christophe, Danovi Davide, Falini Brunangelo, Pelicci Pier Giuseppe, Nucleophosmin regulates the stability and transcriptional activity of p53, 10.1038/ncb814
  5. Colombo E., Bonetti P., Lazzerini Denchi E., Martinelli P., Zamponi R., Marine J.-C., Helin K., Falini B., Pelicci P. G., Nucleophosmin Is Required for DNA Integrity and p19Arf Protein Stability, 10.1128/mcb.25.20.8874-8886.2005
  6. Grisendi Silvia, Mecucci Cristina, Falini Brunangelo, Pandolfi Pier Paolo, Nucleophosmin and cancer, 10.1038/nrc1885
  7. Koike A., Nishikawa H., Wu W., Okada Y., Venkitaraman A. R., Ohta T., Recruitment of Phosphorylated NPM1 to Sites of DNA Damage through RNF8-Dependent Ubiquitin Conjugates, 10.1158/0008-5472.can-10-0382
  8. Poletto M., Lirussi L., Wilson D. M., Tell G., Nucleophosmin modulates stability, activity, and nucleolar accumulation of base excision repair proteins, 10.1091/mbc.e13-12-0717
  9. Namboodiri V.M.Haridasan, Akey Ildikó V., Schmidt-Zachmann Marion S., Head James F., Akey Christopher W., The Structure and Function of Xenopus NO38-Core, a Histone Chaperone in the Nucleolus, 10.1016/j.str.2004.09.017
  10. Lee Hyung Ho, Kim Hyoun Sook, Kang Ji Yong, Lee Byung Il, Ha Jun Yong, Yoon Hye Jin, Lim Seung Oe, Jung Guhung, Suh Se Won, Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface, 10.1002/prot.21504
  11. Grummitt Charles G., Townsley Fiona M., Johnson Christopher M., Warren Alan J., Bycroft Mark, Structural Consequences of Nucleophosmin Mutations in Acute Myeloid Leukemia, 10.1074/jbc.m801706200
  12. Emmott Edward, Hiscox Julian A, Nucleolar targeting: the hub of the matter, 10.1038/embor.2009.14
  13. D Wang, J Biol Chem, 269, 30994 (1994)
  14. Federici Luca, Arcovito Alessandro, Scaglione Giovanni L., Scaloni Flavio, Lo Sterzo Carlo, Di Matteo Adele, Falini Brunangelo, Giardina Bruno, Brunori Maurizio, Nucleophosmin C-terminal Leukemia-associated Domain Interacts with G-rich Quadruplex Forming DNA, 10.1074/jbc.m110.166736
  15. Borer R.A., Lehner C.F., Eppenberger H.M., Nigg E.A., Major nucleolar proteins shuttle between nucleus and cytoplasm, 10.1016/0092-8674(89)90241-9
  16. NISHIMURA Yuki, OHKUBO Takeshi, FURUICHI Yukio, UMEKAWA Hayato, Tryptophans 286 and 288 in the C-terminal Region of Protein B23.1 are Important for Its Nucleolar Localization, 10.1271/bbb.66.2239
  17. Chiarella Sara, De Cola Antonella, Scaglione Giovanni Luca, Carletti Erminia, Graziano Vincenzo, Barcaroli Daniela, Lo Sterzo Carlo, Di Matteo Adele, Di Ilio Carmine, Falini Brunangelo, Arcovito Alessandro, De Laurenzi Vincenzo, Federici Luca, Nucleophosmin mutations alter its nucleolar localization by impairing G-quadruplex binding at ribosomal DNA, 10.1093/nar/gkt001
  18. Yu Y., Maggi L. B., Brady S. N., Apicelli A. J., Dai M.-S., Lu H., Weber J. D., Nucleophosmin Is Essential for Ribosomal Protein L5 Nuclear Export, 10.1128/mcb.26.10.3798-3809.2006
  19. Fung Ho Yee Joyce, Chook Yuh Min, Atomic basis of CRM1-cargo recognition, release and inhibition, 10.1016/j.semcancer.2014.03.002
  20. Kutay Ulrike, Güttinger Stephan, Leucine-rich nuclear-export signals: born to be weak, 10.1016/j.tcb.2005.01.005
  21. Dong Xiuhua, Biswas Anindita, Süel Katherine E., Jackson Laurie K., Martinez Rita, Gu Hongmei, Chook Yuh Min, Structural basis for leucine-rich nuclear export signal recognition by CRM1, 10.1038/nature07975
  22. Monecke T., Guttler T., Neumann P., Dickmanns A., Gorlich D., Ficner R., Crystal Structure of the Nuclear Export Receptor CRM1 in Complex with Snurportin1 and RanGTP, 10.1126/science.1173388
  23. Güttler Thomas, Madl Tobias, Neumann Piotr, Deichsel Danilo, Corsini Lorenzo, Monecke Thomas, Ficner Ralf, Sattler Michael, Görlich Dirk, NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1, 10.1038/nsmb.1931
  24. Bolli N., Nicoletti I., De Marco M. F., Bigerna B., Pucciarini A., Mannucci R., Martelli M. P., Liso A., Mecucci C., Fabbiano F., Martelli M. F., Henderson B. R., Falini B., Born to Be Exported: COOH-Terminal Nuclear Export Signals of Different Strength Ensure Cytoplasmic Accumulation of Nucleophosmin Leukemic Mutants, 10.1158/0008-5472.can-07-0273
  25. Xu D., Farmer A., Collett G., Grishin N. V., Chook Y. M., Sequence and structural analyses of nuclear export signals in the NESdb database, 10.1091/mbc.e12-01-0046
  26. Mitrea D. M., Grace C. R., Buljan M., Yun M.-K., Pytel N. J., Satumba J., Nourse A., Park C.-G., Madan Babu M., White S. W., Kriwacki R. W., Structural polymorphism in the N-terminal oligomerization domain of NPM1, 10.1073/pnas.1321007111
  27. Falini Brunangelo, Mecucci Cristina, Tiacci Enrico, Alcalay Myriam, Rosati Roberto, Pasqualucci Laura, La Starza Roberta, Diverio Daniela, Colombo Emanuela, Santucci Antonella, Bigerna Barbara, Pacini Roberta, Pucciarini Alessandra, Liso Arcangelo, Vignetti Marco, Fazi Paola, Meani Natalia, Pettirossi Valentina, Saglio Giuseppe, Mandelli Franco, Lo-Coco Francesco, Pelicci Pier-Giuseppe, Martelli Massimo F., Cytoplasmic Nucleophosmin in Acute Myelogenous Leukemia with a Normal Karyotype, 10.1056/nejmoa041974
  28. Federici Luca, Falini Brunangelo, Nucleophosmin mutations in acute myeloid leukemia: A tale of protein unfolding and mislocalization, 10.1002/pro.2240
  29. Cheng K., Sportoletti P., Ito K., Clohessy J. G., Teruya-Feldstein J., Kutok J. L., Pandolfi P. P., The cytoplasmic NPM mutant induces myeloproliferation in a transgenic mouse model, 10.1182/blood-2009-03-208587
  30. Bolli N., Payne E. M., Grabher C., Lee J. S., Johnston A. B., Falini B., Kanki J. P., Look A. T., Expression of the cytoplasmic NPM1 mutant (NPMc+) causes the expansion of hematopoietic cells in zebrafish, 10.1182/blood-2009-02-207225
  31. Bañuelos Sonia, Lectez Benoît, Taneva Stefka G., Ormaza Georgina, Alonso-Mariño Marián, Calle Xabier, Urbaneja María A., Recognition of intermolecular G-quadruplexes by full length nucleophosmin. Effect of a leukaemia-associated mutation, 10.1016/j.febslet.2013.05.055
  32. Etchin J, Sun Q, Kentsis A, Farmer A, Zhang Z C, Sanda T, Mansour M R, Barcelo C, McCauley D, Kauffman M, Shacham S, Christie A L, Kung A L, Rodig S J, Chook Y M, Look A T, Antileukemic activity of nuclear export inhibitors that spare normal hematopoietic cells, 10.1038/leu.2012.219
  33. Falini B., Both carboxy-terminus NES motif and mutated tryptophan(s) are crucial for aberrant nuclear export of nucleophosmin leukemic mutants in NPMc+ AML, 10.1182/blood-2005-11-4745
  34. Fox Abigail M., Ciziene Danguole, McLaughlin Stephen H., Stewart Murray, Electrostatic Interactions Involving the Extreme C Terminus of Nuclear Export Factor CRM1 Modulate Its Affinity for Cargo, 10.1074/jbc.m111.245092
  35. Itahana Koji, Bhat Krishna P., Jin Aiwen, Itahana Yoko, Hawke David, Kobayashi Ryuji, Zhang Yanping, Tumor Suppressor ARF Degrades B23, a Nucleolar Protein Involved in Ribosome Biogenesis and Cell Proliferation, 10.1016/s1097-2765(03)00431-3
  36. Rodrı́guez Jose A., Henderson Beric R., Identification of a Functional Nuclear Export Sequence in BRCA1, 10.1074/jbc.m003851200
  37. JA Rodríguez, Oncogene 2006, 25, 4867 (2006)
  38. Henderson Beric R., Eleftheriou Alexandra, A Comparison of the Activity, Sequence Specificity, and CRM1-Dependence of Different Nuclear Export Signals, 10.1006/excr.2000.4825
  39. Koyama Masako, Matsuura Yoshiyuki, An allosteric mechanism to displace nuclear export cargo from CRM1 and RanGTP by RanBP1, 10.1038/emboj.2010.89
  40. Falces Jorge, Arregi Igor, Konarev Petr V., Urbaneja María A., Svergun Dmitri I., Taneva Stefka G., Bañuelos Sonia, Recognition of Nucleoplasmin by Its Nuclear Transport Receptor Importin α/β: Insights into a Complete Import Complex, 10.1021/bi101179g
  41. Dian Cyril, Bernaudat Florent, Langer Karla, Oliva Mizar F., Fornerod Maarten, Schoehn Guy, Müller Christoph W., Petosa Carlo, Structure of a Truncation Mutant of the Nuclear Export Factor CRM1 Provides Insights into the Auto-Inhibitory Role of Its C-Terminal Helix, 10.1016/j.str.2013.06.003
  42. Prieto Gorka, Fullaondo Asier, Rodriguez Jose A., Prediction of nuclear export signals using weighted regular expressions (Wregex), 10.1093/bioinformatics/btu016
  43. Negi Sandeep S., Olson Mark O. J., Effects of interphase and mitotic phosphorylation on the mobility and location of nucleolar protein B23, 10.1242/jcs.03090
  44. Azmi Asfar S., The evolving role of nuclear transporters in cancer, 10.1016/j.semcancer.2014.04.011