Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex

Molecular Cell

Volumn 16, Issue 5, 2004, Pages 761-775

  Petosa, Carlo ^a   Schoehn, Guy ^a,b,c   Askjaer, Peter ^d   Bauer, Ulrike ^d   Moulin, Martine ^a   Steuerwald, Ulrich ^a   Soler López, Montserrat ^a   Baudin, Florence ^a,b,c   Mattaj, Iain W ^d   Müller, Christoph W ^a  

^a EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^b UNIV GRENOBLE ALPES   (France)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; EXPORTIN 1; LEPTOMYCIN B; RAN PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; ELECTRON MICROSCOPY; MOLECULAR MODEL; MOLECULAR RECOGNITION; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN STRUCTURE; PROTEIN TARGETING; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID SEQUENCE; BETA KARYOPHERINS; BINDING SITES; CELL NUCLEUS; CRYSTALLOGRAPHY, X-RAY; DOSE-RESPONSE RELATIONSHIP, DRUG; FATTY ACIDS, UNSATURATED; GTP PHOSPHOHYDROLASES; GUANOSINE TRIPHOSPHATE; HUMANS; IMAGE PROCESSING, COMPUTER-ASSISTED; KARYOPHERINS; LEUCINE; MICROSCOPY, ELECTRON; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; RAN GTP-BINDING PROTEIN; RECEPTORS, CYTOPLASMIC AND NUCLEAR; SEQUENCE HOMOLOGY, AMINO ACID;

NES;

EID: 9744248734     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.11.018     Document Type: Article

References (53)

1. Andrade M.A., Bork P. HEAT repeats in the Huntington's disease protein. Nat. Genet. 11:1995;115-116
2. Andrade M.A., Petosa C., O'Donoghue S.I., Müller C.W., Bork P. Comparison of ARM and HEAT protein repeats. J. Mol. Biol. 309:2001;1-18
3. Askjaer P., Bachi A., Wilm M., Bischoff F.R., Weeks D.L., Ogniewski V., Ohno M., Niehrs C., Kjems J., Mattaj I.W., Fornerod M. RanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase. Mol. Cell. Biol. 19:1999;6276-6285
4. Bayliss R., Littlewood T., Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell. 102:2000;99-108
5. Bayliss R., Leung S.W., Baker R.P., Quimby B.B., Corbett A.H., Stewart M. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21:2002;2843-2853
6. Brünger A.T., Adams P.D., Clore G.M., Gros P., Grosse-Juntsleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., et al. Crystallography and NMR system. a new software system for macromolecular structure determination Acta Crystallogr. D. 54:1998;905-921
7. CCP4 The CCP4 (Collaborative Computational Project Number 4) suite. programs for protein crystallography Acta Crystallogr. D. Biol. Crystallogr. 50:1994;760-763
8. Chacón P., Wriggers W. Multi-resolution contour-based fitting of macromolecular structures. J. Mol. Biol. 317:2002;375-384
9. Chook Y.M., Blobel G. Structure of the nuclear transport complex karyopherin-beta2-RanGppNHp. Nature. 399:1999;230-237
10. Chook Y.M., Blobel G. Karyopherins and nuclear import. Curr. Opin. Struct. Biol. 11:2001;703-715
11. Chook Y.M., Jung A., Rosen M.K., Blobel G. Uncoupling Kapbeta2 substrate dissociation and Ran binding. Biochemistry. 41:2002;6955-6966
12. Cingolani G., Petosa C., Weis K., Müller C.W. Structure of importin-beta bound to the IBB domain of importin-alpha. Nature. 399:1999;221-229
13. Cingolani G., Bednenko J., Gillespie M.T., Gerace L. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta. Mol. Cell. 10:2002;1345-1353
14. Conway J.F., Steven A.C. Methods for reconstructing density maps of "single" particles from cryoelectron micrographs to subnanometer resolution. J. Struct. Biol. 128:1999;106-118
15. de La Fortelle E., Bricogne G. Maximum-likelihood heavy-atom parameter refinement in the MIR and MAD methods. Meth. Enzymol. 276:1997;472-494
16. Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2:2001;926-932
17. Fischer U., Huber J., Boelens W.C., Mattaj I.W., Luhrmann R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 82:1995;475-483
18. Fornerod M., Ohno M., Yoshida M., Mattaj I.W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 90:1997;1051-1060. a
19. Fornerod M., van Deursen J., van Baal S., Reynolds A., Davis D., Murti K.G., Fransen J., Grosveld G. The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J. 16:1997;807-816. b
20. Frank J., Radermacher M., Penczek P., Zhu J., Li Y., Ladjadj M., Leith A. Spider and web. processing and visualization of images in 3D electron microscopy and related fields J. Struct. Biol. 116:1996;190-199
21. Fried H., Kutay U. Nucleocytoplasmic transport. taking an inventory Cell. Mol. Life Sci. 60:2003;1659-1688
22. 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. 390:1997;308-311
23. Fukuhara N., Fernandez E., Ebert J., Conti E., Svergun D. Conformational variability of nucleo-cytoplasmic transport factors. J. Biol. Chem. 279:2004;2176-2181
24. Görlich D., Dabrowski M., Bischoff F.R., Kutay U., Bork P., Hartmann E., Prehn S., Izaurralde E. A novel class of RanGTP binding proteins. J. Cell Biol. 138:1997;65-80
25. Hakata Y., Yamada M., Shida H. A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein. Mol. Cell. Biol. 23:2003;8751-8761
26. Holaska J.M., Paschal B.M. A cytosolic activity distinct from crm1 mediates nuclear export of protein kinase inhibitor in permeabilized cells. Proc. Natl. Acad. Sci. USA. 95:1998;14739-14744
27. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119
28. Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26:1993;795-800
29. Kudo N., Matsumori N., Taoka H., Fujiwara D., Schreiner E.P., Wolff B., Yoshida M., Horinouchi S. Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc. Natl. Acad. Sci. USA. 96:1999;9112-9117
30. la Cour T., Gupta R., Rapacki K., Skriver K., Poulsen F.M., Brunak S. NESbase version 1.0. a database of nuclear export signals Nucleic Acids Res. 31:2003;393-396
31. Laskowski R.A., MacArthur M.W., Moss D.S., Thornton J.M. Procheck. a program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26:1993;283-291
32. Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J. Cell Biol. 153:2001;1391-1402
33. Lee S.J., Sekimoto T., Yamashita E., Nagoshi E., Nakagawa A., Imamoto N., Yoshimura M., Sakai H., Chong K.T., Tsukihara T., Yoneda Y. The structure of importin-β bound to SREBP-2. nuclear import of a transcription factor Science. 302:2003;1571-1575
34. Nishi K., Yoshida M., Fujiwara D., Nishikawa M., Horinouchi S., Beppu T. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J. Biol. Chem. 269:1994;6320-6324
35. Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W. PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation. Cell. 101:2000;187-198
36. Ossareh-Nazari B., Dargemont C. Domains of Crm1 involved in the formation of the Crm1, RanGTP and leucine-rich nuclear export sequences trimeric complex. Exp. Cell Res. 252:1999;236-241
37. Ossareh-Nazari B., Bacheleri F., Dargemont C. Evidence for a role of crm1 in signal-mediated nuclear protein export. Science. 278:1997;141-144
38. Paraskeva E., Izzauralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luhrmann R., Görlich D. CRM1-mediated recycling of snurportin 1 to the cytoplasm. J. Cell Biol. 145:1999;255-264
39. Park J., Teichmann S.A., Hubbard T., Chothia C. Intermediate sequences increase the detection of homology between sequences. J. Mol. Biol. 273:1997;349-354
40. Roseman A.M., Chen S., White H., Braig K., Saibil H.R. The chaperonin ATPase cycle. mechanism of allosteric switching and movements of substrate-binding domains in GroEl Cell. 87:1996;241-251
41. Sali A., Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:1993;779-815
42. Schneider T.R., Sheldrick G.M. Substructure solution with SHELXD. Acta Crystallogr. D Biol. Crystallogr. 58:2002;1772-1779
43. Schoehn G., Quaite-Randall E., Jiménez J.L., Joachimiak A., Saibil H. Three conformations of an archeal chaperonin, TF55 from Sulfolobus shibatae. J. Mol. Biol. 296:2000;813-819
44. Schuler G.D., Altschul S.F., Lipman D.J. A workbench for multiple alignment construction and analysis. Proteins. 9:1991;180-190
45. Stade K., Ford C.S., Guthrie C., Weis K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell. 90:1997;1041-1050
46. Tatusova T.A., Madden T.L. BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences. FEMS Microbiol. Lett. 174:1999;247-250
47. Terwilliger T.C. Maximum likelihood density modification. Acta Crystallogr. D Biol. Crystallogr. 56:2000;965-972
48. Vetter I.R., Arndt A., Kutay U., Görlich D., Wittinghofer A. Structural view of the Ran-Importin beta interaction at 2.3 A resolution. Cell. 97:1999;635-646
49. Vriend G. What if. a molecular modeling and drug design program J. Mol. Graph. 8:1990;52-56
50. Weis K. Regulating access to the genome. nucleocytoplasmic transport throughout the cell cycle Cell. 112:2003;441-451
51. Wen W., Meinkoth J.L., Tsien R.Y., Taylor S.S. Identification of a signal for rapid export of proteins from the nucleus. Cell. 82:1995;463-473
52. Wolff B., Sanglier J.J., Wang Y. Leptomycin B is an inhibitor of nuclear export. inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA Chem. Biol. 4:1997;139-147
53. Zampighi G.A., Kreman M., Lanzavecchia S., Turk E., Eskandari E., Zampighi L., Wright E.M. Structure of functional AQP0 channels in phospholipid bilayers. J. Mol. Biol. 325:2003;201-210