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Wikipedia

XPO1

December 15, 2023

Exportin 1 (XPO1), also known as chromosomal region maintenance 1 (CRM1), is a eukaryotic protein that mediates the nuclear export of various proteins and RNAs.

XPO1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesXPO1, CRM1, emb, exp1, exportin 1, CRM-1
External IDsOMIM: 602559 MGI: 2144013 HomoloGene: 2554 GeneCards: XPO1
Orthologs
SpeciesHumanMouse
Entrez

7514

103573

Ensembl

ENSG00000082898

ENSMUSG00000020290

UniProt

O14980

Q6P5F9

RefSeq (mRNA)

NM_003400

NM_001035226
NM_134014

RefSeq (protein)

NP_003391

NP_001030303
NP_598775

Location (UCSC)Chr 2: 61.48 – 61.54 MbChr 11: 23.21 – 23.25 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

History edit

XPO1 (CRM1) originally was identified in the fission yeast Schizosaccharomyces pombe in a genetic screen, and investigators determined that it was involved in control of the chromosome structure.[5] It was later shown to be the nuclear transport receptor for cargos with leucine-rich nuclear export signals (NES).[6][7][8][9] The structural details of the interaction of XPO1 with its cargos were revealed two decades after the gene was identified.[10][11][12][13]

Function edit

XPO1 mediates NES-dependent protein transport. It exports several hundreds of different proteins from the nucleus.[14][15] XPO1 is involved in the nuclear export of ribosomal subunits.[16][17][18] XPO1 plays a role in export of various RNAs including U snRNAs, rRNAs (as a part of ribosomal subunits), and some mRNAs.[19][20][21]

Medical relevance edit

XPO1 is involved in various viral infections. For example, it is required for the nuclear export of HIV-1 RNA in complex with the viral protein Rev, an event that is a crucial part of the infection cycle.[22] XPO1 is affected in some cancer types [23] and is therefore viewed as a target for development of anti-cancer drugs.[24] Selinexor, a drug specifically targeting XPO1, was approved by the FDA for treatment of multiple myeloma.[25]

Interactions edit

XPO1 has been shown to interact with:

See also edit

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000082898 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020290 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Adachi, Y.; Yanagida, M. (1989-04-01). "Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein preferentially localized in the nucleus and its periphery". Journal of Cell Biology. 108 (4): 1195–1207. doi:10.1083/jcb.108.4.1195. ISSN 0021-9525. PMC 2115495. PMID 2647765.
  6. ^ Fornerod, M.; Ohno, M.; Yoshida, M.; Mattaj, I. W. (1997-09-19). "CRM1 is an export receptor for leucine-rich nuclear export signals". Cell. 90 (6): 1051–1060. doi:10.1016/s0092-8674(00)80371-2. ISSN 0092-8674. PMID 9323133.
  7. ^ Fukuda, M.; Asano, S.; Nakamura, T.; Adachi, M.; Yoshida, M.; Yanagida, M.; Nishida, E. (1997-11-20). "CRM1 is responsible for intracellular transport mediated by the nuclear export signal". Nature. 390 (6657): 308–311. Bibcode:1997Natur.390..308F. doi:10.1038/36894. ISSN 0028-0836. PMID 9384386. S2CID 4420607.
  8. ^ Stade, K.; Ford, C. S.; Guthrie, C.; Weis, K. (1997-09-19). "Exportin 1 (Crm1p) is an essential nuclear export factor". Cell. 90 (6): 1041–1050. doi:10.1016/s0092-8674(00)80370-0. ISSN 0092-8674. PMID 9323132.
  9. ^ Ossareh-Nazari, B.; Bachelerie, F.; Dargemont, C. (1997-10-03). "Evidence for a role of CRM1 in signal-mediated nuclear protein export". Science. 278 (5335): 141–144. doi:10.1126/science.278.5335.141. ISSN 0036-8075. PMID 9311922.
  10. ^ Monecke, Thomas; Güttler, Thomas; Neumann, Piotr; Dickmanns, Achim; Görlich, Dirk; Ficner, Ralf (2009-05-22). "Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP". Science. 324 (5930): 1087–1091. Bibcode:2009Sci...324.1087M. doi:10.1126/science.1173388. ISSN 1095-9203. PMID 19389996. S2CID 21116091.
  11. ^ Dong, Xiuhua; Biswas, Anindita; Süel, Katherine E.; Jackson, Laurie K.; Martinez, Rita; Gu, Hongmei; Chook, Yuh Min (2009-04-30). "Structural basis for leucine-rich nuclear export signal recognition by CRM1". Nature. 458 (7242): 1136–1141. Bibcode:2009Natur.458.1136D. doi:10.1038/nature07975. ISSN 1476-4687. PMC 3437623. PMID 19339969.
  12. ^ Dong, Xiuhua; Biswas, Anindita; Chook, Yuh Min (May 2009). "Structural basis for assembly and disassembly of the CRM1 nuclear export complex". Nature Structural & Molecular Biology. 16 (5): 558–560. doi:10.1038/nsmb.1586. ISSN 1545-9985. PMC 3437629. PMID 19339972.
  13. ^ Güttler, Thomas; Madl, Tobias; Neumann, Piotr; Deichsel, Danilo; Corsini, Lorenzo; Monecke, Thomas; Ficner, Ralf; Sattler, Michael; Görlich, Dirk (November 2010). "NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1". Nature Structural & Molecular Biology. 17 (11): 1367–1376. doi:10.1038/nsmb.1931. hdl:11858/00-001M-0000-0012-D4DB-B. ISSN 1545-9985. PMID 20972448. S2CID 21593381.
  14. ^ Thakar, Ketan; Karaca, Samir; Port, Sarah A.; Urlaub, Henning; Kehlenbach, Ralph H. (March 2013). "Identification of CRM1-dependent Nuclear Export Cargos Using Quantitative Mass Spectrometry". Molecular & Cellular Proteomics. 12 (3): 664–678. doi:10.1074/mcp.M112.024877. ISSN 1535-9484. PMC 3591659. PMID 23242554.
  15. ^ Kırlı, Koray; Karaca, Samir; Dehne, Heinz Jürgen; Samwer, Matthias; Pan, Kuan Ting; Lenz, Christof; Urlaub, Henning; Görlich, Dirk (2015-12-17). "A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning". eLife. 4. doi:10.7554/eLife.11466. ISSN 2050-084X. PMC 4764573. PMID 26673895.
  16. ^ Moy, T. I.; Silver, P. A. (1999-08-15). "Nuclear export of the small ribosomal subunit requires the ran-GTPase cycle and certain nucleoporins". Genes & Development. 13 (16): 2118–2133. doi:10.1101/gad.13.16.2118. ISSN 0890-9369. PMC 316945. PMID 10465789.
  17. ^ Ho, J. H.; Kallstrom, G.; Johnson, A. W. (2000-11-27). "Nmd3p is a Crm1p-dependent adapter protein for nuclear export of the large ribosomal subunit". The Journal of Cell Biology. 151 (5): 1057–1066. doi:10.1083/jcb.151.5.1057. ISSN 0021-9525. PMC 2174350. PMID 11086007.
  18. ^ Zemp, Ivo; Wild, Thomas; O'Donohue, Marie-Françoise; Wandrey, Franziska; Widmann, Barbara; Gleizes, Pierre-Emmanuel; Kutay, Ulrike (2009-06-29). "Distinct cytoplasmic maturation steps of 40S ribosomal subunit precursors require hRio2". The Journal of Cell Biology. 185 (7): 1167–1180. doi:10.1083/jcb.200904048. ISSN 1540-8140. PMC 2712965. PMID 19564402.
  19. ^ Cullen, B. R. (June 2000). "Nuclear RNA export pathways". Molecular and Cellular Biology. 20 (12): 4181–4187. doi:10.1128/mcb.20.12.4181-4187.2000. ISSN 0270-7306. PMC 85787. PMID 10825183.
  20. ^ Köhler, Alwin; Hurt, Ed (October 2007). "Exporting RNA from the nucleus to the cytoplasm". Nature Reviews Molecular Cell Biology. 8 (10): 761–773. doi:10.1038/nrm2255. ISSN 1471-0080. PMID 17786152. S2CID 10836137.
  21. ^ Sloan, Katherine E.; Gleizes, Pierre-Emmanuel; Bohnsack, Markus T. (2016-05-22). "Nucleocytoplasmic Transport of RNAs and RNA–Protein Complexes". Journal of Molecular Biology. 428 (10): 2040–2059. doi:10.1016/j.jmb.2015.09.023. ISSN 0022-2836. PMID 26434509.
  22. ^ Booth, David S; Cheng, Yifan; Frankel, Alan D (2014-12-08). Sundquist, Wesley I (ed.). "The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA". eLife. 3: e04121. doi:10.7554/eLife.04121. ISSN 2050-084X. PMC 4360530. PMID 25486595.
  23. ^ Taylor, Justin; Sendino, Maria; Gorelick, Alexander N.; Pastore, Alessandro; Chang, Matthew T.; Penson, Alexander V.; Gavrila, Elena I.; Stewart, Connor; Melnik, Ella M.; Herrejon Chavez, Florisela; Bitner, Lillian (October 2019). "Altered Nuclear Export Signal Recognition as a Driver of Oncogenesis". Cancer Discovery. 9 (10): 1452–1467. doi:10.1158/2159-8290.CD-19-0298. ISSN 2159-8290. PMC 6774834. PMID 31285298.
  24. ^ Fung, Ho Yee Joyce; Chook, Yuh Min (August 2014). "Atomic basis of CRM1-cargo recognition, release and inhibition". Seminars in Cancer Biology. 27: 52–61. doi:10.1016/j.semcancer.2014.03.002. ISSN 1096-3650. PMC 4108548. PMID 24631835.
  25. ^ Research, Center for Drug Evaluation and (2019-12-20). "FDA grants accelerated approval to selinexor for multiple myeloma". FDA.
  26. ^ a b Tickenbrock L, Cramer J, Vetter IR, Muller O (August 2002). "The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1)". J. Biol. Chem. 277 (35): 32332–8. doi:10.1074/jbc.M203990200. PMID 12070164.
  27. ^ Ishida N, Hara T, Kamura T, Yoshida M, Nakayama K, Nakayama KI (April 2002). "Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export". J. Biol. Chem. 277 (17): 14355–8. doi:10.1074/jbc.C100762200. PMID 11889117.
  28. ^ Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG, Melchior F, Hengst L, Slingerland JM (January 2003). "CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis". Mol. Biol. Cell. 14 (1): 201–13. doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437.
  29. ^ Raval A, Weissman JD, Howcroft TK, Singer DS (January 2003). "The GTP-binding domain of class II transactivator regulates its nuclear export". J. Immunol. 170 (2): 922–30. doi:10.4049/jimmunol.170.2.922. PMID 12517958.
  30. ^ Voong LN, Slater AR, Kratovac S, Cressman DE (April 2008). "Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator". J. Biol. Chem. 283 (14): 9031–9. doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089.
  31. ^ Thomas F, Kutay U (June 2003). "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway". J. Cell Sci. 116 (Pt 12): 2409–19. doi:10.1242/jcs.00464. PMID 12724356.
  32. ^ a b Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG (June 2001). "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export". J. Cell Biol. 153 (7): 1391–402. doi:10.1083/jcb.153.7.1391. PMC 2150735. PMID 11425870.
  33. ^ Kehlenbach RH, Dickmanns A, Kehlenbach A, Guan T, Gerace L (May 1999). "A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export". J. Cell Biol. 145 (4): 645–57. doi:10.1083/jcb.145.4.645. PMC 2133185. PMID 10330396.
  34. ^ a b Plafker K, Macara IG (May 2000). "Facilitated nucleocytoplasmic shuttling of the Ran binding protein RanBP1". Mol. Cell. Biol. 20 (10): 3510–21. doi:10.1128/mcb.20.10.3510-3521.2000. PMC 85643. PMID 10779340.
  35. ^ Singh BB, Patel HH, Roepman R, Schick D, Ferreira PA (Dec 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem. 274 (52): 37370–8. doi:10.1074/jbc.274.52.37370. PMID 10601307.
  36. ^ Lindsay ME, Plafker K, Smith AE, Clurman BE, Macara IG (August 2002). "Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import". Cell. 110 (3): 349–60. doi:10.1016/s0092-8674(02)00836-x. PMID 12176322. S2CID 15515037.
  37. ^ Fornerod M, Ohno M, Yoshida M, Mattaj IW (September 1997). "CRM1 is an export receptor for leucine-rich nuclear export signals". Cell. 90 (6): 1051–60. doi:10.1016/s0092-8674(00)80371-2. PMID 9323133. S2CID 15119502.
  38. ^ Craig E, Zhang ZK, Davies KP, Kalpana GV (January 2002). "A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis". EMBO J. 21 (1–2): 31–42. doi:10.1093/emboj/21.1.31. PMC 125819. PMID 11782423.
  39. ^ Kanai M, Hanashiro K, Kim SH, Hanai S, Boulares AH, Miwa M, Fukasawa K (September 2007). "Inhibition of Crm1-p53 interaction and nuclear export of p53 by poly(ADP-ribosyl)ation". Nat. Cell Biol. 9 (10): 1175–83. doi:10.1038/ncb1638. PMID 17891139. S2CID 13433567.
  40. ^ Shao C, Lu C, Chen L, Koty PP, Cobos E, Gao W (August 2010). "p53-Dependent anticancer effects of leptomycin B on lung adenocarcinoma". Cancer Chemother. Pharmacol. 67 (6): 1369–80. doi:10.1007/s00280-010-1434-6. PMID 20803015. S2CID 27127578.

Further reading edit

  • Görlich D, Kutay U (1999). "Transport between the cell nucleus and the cytoplasm". Annu. Rev. Cell Dev. Biol. 15 (1): 607–60. doi:10.1146/annurev.cellbio.15.1.607. PMID 10611974.
  • Budhu AS, Wang XW (2007). "Loading and unloading: orchestrating centrosome duplication and spindle assembly by Ran/Crm1". Cell Cycle. 4 (11): 1510–4. doi:10.4161/cc.4.11.2187. PMC 1402358. PMID 16294017.
  • Li L, Li HS, Pauza CD, Bukrinsky M, Zhao RY (2006). "Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions". Cell Res. 15 (11–12): 923–34. doi:10.1038/sj.cr.7290370. PMID 16354571.
  • Stauber RH, Mann W, Knauer SK (2007). "Nuclear and cytoplasmic survivin: molecular mechanism, prognostic, and therapeutic potential". Cancer Res. 67 (13): 5999–6002. doi:10.1158/0008-5472.CAN-07-0494. PMID 17616652.
  • Mathew C, Ghildyal R (2017). "CRM1 inhibitors for antiviral therapy". Frontiers in Microbiology. 8: 1171. doi:10.3389/fmicb.2017.01171. PMC 5487384. PMID 28702009.

External links edit

  • 3D electron microscopy structures of CRM1 from the EM Data Bank(EMDB)


 

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December 15, 2023
xpo1, exportin, also, known, chromosomal, region, maintenance, crm1, eukaryotic, protein, that, mediates, nuclear, export, various, proteins, rnas, available, structurespdbortholog, search, pdbe, rcsblist, codes1w9c, 2l1l, 3gb8, 4bsm, 4bsn, 5disidentifiersalia. Exportin 1 XPO1 also known as chromosomal region maintenance 1 CRM1 is a eukaryotic protein that mediates the nuclear export of various proteins and RNAs XPO1Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes1W9C 2L1L 3GB8 4BSM 4BSN 5DISIdentifiersAliasesXPO1 CRM1 emb exp1 exportin 1 CRM 1External IDsOMIM 602559 MGI 2144013 HomoloGene 2554 GeneCards XPO1Gene location Human Chr Chromosome 2 human 1 Band2p15Start61 476 032 bp 1 End61 538 741 bp 1 Gene location Mouse Chr Chromosome 11 mouse 2 Band11 11 A3 2Start23 206 041 bp 2 End23 248 249 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed intibiagerminal epitheliumparietal pleuravisceral pleuraembryospongy bonepalpebral conjunctivaganglionic eminenceretinal pigment epitheliumsuperficial temporal arteryTop expressed inprimitive streakdermisabdominal wallmedullary collecting ductmaxillary prominencerenal corpusclesomitecumulus cellmedial ganglionic eminencevas deferensMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein domain specific binding transporter activity protein binding RNA binding structural constituent of nuclear pore nuclear export signal receptor activityCellular componentcytoplasm Cajal body nuclear membrane membrane intracellular membrane bounded organelle nuclear envelope nucleoplasm lamellae anulatae nucleus kinetochore nucleolus cytosol host cell protein containing complex ribonucleoprotein complex intracellular anatomical structureBiological processribosomal small subunit export from nucleus intracellular transport of virus regulation of centrosome duplication mRNA transport regulation of mRNA stability negative regulation of transcription by RNA polymerase II protein export from nucleus regulation of protein catabolic process protein localization to nucleus protein transport ribosomal large subunit export from nucleus intracellular protein transport viral process sister chromatid cohesion ribosomal subunit export from nucleus regulation of protein export from nucleus ribosome biogenesis transport nucleocytoplasmic transportSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez7514103573EnsemblENSG00000082898ENSMUSG00000020290UniProtO14980Q6P5F9RefSeq mRNA NM 003400NM 001035226NM 134014RefSeq protein NP 003391NP 001030303NP 598775Location UCSC Chr 2 61 48 61 54 MbChr 11 23 21 23 25 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 History 2 Function 3 Medical relevance 4 Interactions 5 See also 6 References 7 Further reading 8 External linksHistory editXPO1 CRM1 originally was identified in the fission yeast Schizosaccharomyces pombe in a genetic screen and investigators determined that it was involved in control of the chromosome structure 5 It was later shown to be the nuclear transport receptor for cargos with leucine rich nuclear export signals NES 6 7 8 9 The structural details of the interaction of XPO1 with its cargos were revealed two decades after the gene was identified 10 11 12 13 Function editXPO1 mediates NES dependent protein transport It exports several hundreds of different proteins from the nucleus 14 15 XPO1 is involved in the nuclear export of ribosomal subunits 16 17 18 XPO1 plays a role in export of various RNAs including U snRNAs rRNAs as a part of ribosomal subunits and some mRNAs 19 20 21 Medical relevance editXPO1 is involved in various viral infections For example it is required for the nuclear export of HIV 1 RNA in complex with the viral protein Rev an event that is a crucial part of the infection cycle 22 XPO1 is affected in some cancer types 23 and is therefore viewed as a target for development of anti cancer drugs 24 Selinexor a drug specifically targeting XPO1 was approved by the FDA for treatment of multiple myeloma 25 Interactions editXPO1 has been shown to interact with APC 26 CDKN1B 27 28 CIITA 29 30 NMD3 31 Nucleoporin 62 32 33 RANBP1 34 35 RANBP3 32 36 Ran 26 34 37 SMARCB1 38 and p53 39 40 See also editKaryopherin Importin Nuclear transport Nuclear export signalReferences edit a b c GRCh38 Ensembl release 89 ENSG00000082898 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000020290 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Adachi Y Yanagida M 1989 04 01 Higher order chromosome structure is affected by cold sensitive mutations in a Schizosaccharomyces pombe gene crm1 which encodes a 115 kD protein preferentially localized in the nucleus and its periphery Journal of Cell Biology 108 4 1195 1207 doi 10 1083 jcb 108 4 1195 ISSN 0021 9525 PMC 2115495 PMID 2647765 Fornerod M Ohno M Yoshida M Mattaj I W 1997 09 19 CRM1 is an export receptor for leucine rich nuclear export signals Cell 90 6 1051 1060 doi 10 1016 s0092 8674 00 80371 2 ISSN 0092 8674 PMID 9323133 Fukuda M Asano S Nakamura T Adachi M Yoshida M Yanagida M Nishida E 1997 11 20 CRM1 is responsible for intracellular transport mediated by the nuclear export signal Nature 390 6657 308 311 Bibcode 1997Natur 390 308F doi 10 1038 36894 ISSN 0028 0836 PMID 9384386 S2CID 4420607 Stade K Ford C S Guthrie C Weis K 1997 09 19 Exportin 1 Crm1p is an essential nuclear export factor Cell 90 6 1041 1050 doi 10 1016 s0092 8674 00 80370 0 ISSN 0092 8674 PMID 9323132 Ossareh Nazari B Bachelerie F Dargemont C 1997 10 03 Evidence for a role of CRM1 in signal mediated nuclear protein export Science 278 5335 141 144 doi 10 1126 science 278 5335 141 ISSN 0036 8075 PMID 9311922 Monecke Thomas Guttler Thomas Neumann Piotr Dickmanns Achim Gorlich Dirk Ficner Ralf 2009 05 22 Crystal structure of the nuclear export receptor CRM1 in complex with Snurportin1 and RanGTP Science 324 5930 1087 1091 Bibcode 2009Sci 324 1087M doi 10 1126 science 1173388 ISSN 1095 9203 PMID 19389996 S2CID 21116091 Dong Xiuhua Biswas Anindita Suel Katherine E Jackson Laurie K Martinez Rita Gu Hongmei Chook Yuh Min 2009 04 30 Structural basis for leucine rich nuclear export signal recognition by CRM1 Nature 458 7242 1136 1141 Bibcode 2009Natur 458 1136D doi 10 1038 nature07975 ISSN 1476 4687 PMC 3437623 PMID 19339969 Dong Xiuhua Biswas Anindita Chook Yuh Min May 2009 Structural basis for assembly and disassembly of the CRM1 nuclear export complex Nature Structural amp Molecular Biology 16 5 558 560 doi 10 1038 nsmb 1586 ISSN 1545 9985 PMC 3437629 PMID 19339972 Guttler Thomas Madl Tobias Neumann Piotr Deichsel Danilo Corsini Lorenzo Monecke Thomas Ficner Ralf Sattler Michael Gorlich Dirk November 2010 NES consensus redefined by structures of PKI type and Rev type nuclear export signals bound to CRM1 Nature Structural amp Molecular Biology 17 11 1367 1376 doi 10 1038 nsmb 1931 hdl 11858 00 001M 0000 0012 D4DB B ISSN 1545 9985 PMID 20972448 S2CID 21593381 Thakar Ketan Karaca Samir Port Sarah A Urlaub Henning Kehlenbach Ralph H March 2013 Identification of CRM1 dependent Nuclear Export Cargos Using Quantitative Mass Spectrometry Molecular amp Cellular Proteomics 12 3 664 678 doi 10 1074 mcp M112 024877 ISSN 1535 9484 PMC 3591659 PMID 23242554 Kirli Koray Karaca Samir Dehne Heinz Jurgen Samwer Matthias Pan Kuan Ting Lenz Christof Urlaub Henning Gorlich Dirk 2015 12 17 A deep proteomics perspective on CRM1 mediated nuclear export and nucleocytoplasmic partitioning eLife 4 doi 10 7554 eLife 11466 ISSN 2050 084X PMC 4764573 PMID 26673895 Moy T I Silver P A 1999 08 15 Nuclear export of the small ribosomal subunit requires the ran GTPase cycle and certain nucleoporins Genes amp Development 13 16 2118 2133 doi 10 1101 gad 13 16 2118 ISSN 0890 9369 PMC 316945 PMID 10465789 Ho J H Kallstrom G Johnson A W 2000 11 27 Nmd3p is a Crm1p dependent adapter protein for nuclear export of the large ribosomal subunit The Journal of Cell Biology 151 5 1057 1066 doi 10 1083 jcb 151 5 1057 ISSN 0021 9525 PMC 2174350 PMID 11086007 Zemp Ivo Wild Thomas O Donohue Marie Francoise Wandrey Franziska Widmann Barbara Gleizes Pierre Emmanuel Kutay Ulrike 2009 06 29 Distinct cytoplasmic maturation steps of 40S ribosomal subunit precursors require hRio2 The Journal of Cell Biology 185 7 1167 1180 doi 10 1083 jcb 200904048 ISSN 1540 8140 PMC 2712965 PMID 19564402 Cullen B R June 2000 Nuclear RNA export pathways Molecular and Cellular Biology 20 12 4181 4187 doi 10 1128 mcb 20 12 4181 4187 2000 ISSN 0270 7306 PMC 85787 PMID 10825183 Kohler Alwin Hurt Ed October 2007 Exporting RNA from the nucleus to the cytoplasm Nature Reviews Molecular Cell Biology 8 10 761 773 doi 10 1038 nrm2255 ISSN 1471 0080 PMID 17786152 S2CID 10836137 Sloan Katherine E Gleizes Pierre Emmanuel Bohnsack Markus T 2016 05 22 Nucleocytoplasmic Transport of RNAs and RNA Protein Complexes Journal of Molecular Biology 428 10 2040 2059 doi 10 1016 j jmb 2015 09 023 ISSN 0022 2836 PMID 26434509 Booth David S Cheng Yifan Frankel Alan D 2014 12 08 Sundquist Wesley I ed The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA eLife 3 e04121 doi 10 7554 eLife 04121 ISSN 2050 084X PMC 4360530 PMID 25486595 Taylor Justin Sendino Maria Gorelick Alexander N Pastore Alessandro Chang Matthew T Penson Alexander V Gavrila Elena I Stewart Connor Melnik Ella M Herrejon Chavez Florisela Bitner Lillian October 2019 Altered Nuclear Export Signal Recognition as a Driver of Oncogenesis Cancer Discovery 9 10 1452 1467 doi 10 1158 2159 8290 CD 19 0298 ISSN 2159 8290 PMC 6774834 PMID 31285298 Fung Ho Yee Joyce Chook Yuh Min August 2014 Atomic basis of CRM1 cargo recognition release and inhibition Seminars in Cancer Biology 27 52 61 doi 10 1016 j semcancer 2014 03 002 ISSN 1096 3650 PMC 4108548 PMID 24631835 Research Center for Drug Evaluation and 2019 12 20 FDA grants accelerated approval to selinexor for multiple myeloma FDA a b Tickenbrock L Cramer J Vetter IR Muller O August 2002 The coiled coil region amino acids 129 250 of the tumor suppressor protein adenomatous polyposis coli APC Its structure and its interaction with chromosome maintenance region 1 Crm 1 J Biol Chem 277 35 32332 8 doi 10 1074 jbc M203990200 PMID 12070164 Ishida N Hara T Kamura T Yoshida M Nakayama K Nakayama KI April 2002 Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export J Biol Chem 277 17 14355 8 doi 10 1074 jbc C100762200 PMID 11889117 Connor MK Kotchetkov R Cariou S Resch A Lupetti R Beniston RG Melchior F Hengst L Slingerland JM January 2003 CRM1 Ran mediated nuclear export of p27 Kip1 involves a nuclear export signal and links p27 export and proteolysis Mol Biol Cell 14 1 201 13 doi 10 1091 mbc E02 06 0319 PMC 140238 PMID 12529437 Raval A Weissman JD Howcroft TK Singer DS January 2003 The GTP binding domain of class II transactivator regulates its nuclear export J Immunol 170 2 922 30 doi 10 4049 jimmunol 170 2 922 PMID 12517958 Voong LN Slater AR Kratovac S Cressman DE April 2008 Mitogen activated protein kinase ERK1 2 regulates the class II transactivator J Biol Chem 283 14 9031 9 doi 10 1074 jbc M706487200 PMC 2431044 PMID 18245089 Thomas F Kutay U June 2003 Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway J Cell Sci 116 Pt 12 2409 19 doi 10 1242 jcs 00464 PMID 12724356 a b Lindsay ME Holaska JM Welch K Paschal BM Macara IG June 2001 Ran binding protein 3 is a cofactor for Crm1 mediated nuclear protein export J Cell Biol 153 7 1391 402 doi 10 1083 jcb 153 7 1391 PMC 2150735 PMID 11425870 Kehlenbach RH Dickmanns A Kehlenbach A Guan T Gerace L May 1999 A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export J Cell Biol 145 4 645 57 doi 10 1083 jcb 145 4 645 PMC 2133185 PMID 10330396 a b Plafker K Macara IG May 2000 Facilitated nucleocytoplasmic shuttling of the Ran binding protein RanBP1 Mol Cell Biol 20 10 3510 21 doi 10 1128 mcb 20 10 3510 3521 2000 PMC 85643 PMID 10779340 Singh BB Patel HH Roepman R Schick D Ferreira PA Dec 1999 The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor exportin 1 J Biol Chem 274 52 37370 8 doi 10 1074 jbc 274 52 37370 PMID 10601307 Lindsay ME Plafker K Smith AE Clurman BE Macara IG August 2002 Npap60 Nup50 is a tri stable switch that stimulates importin alpha beta mediated nuclear protein import Cell 110 3 349 60 doi 10 1016 s0092 8674 02 00836 x PMID 12176322 S2CID 15515037 Fornerod M Ohno M Yoshida M Mattaj IW September 1997 CRM1 is an export receptor for leucine rich nuclear export signals Cell 90 6 1051 60 doi 10 1016 s0092 8674 00 80371 2 PMID 9323133 S2CID 15119502 Craig E Zhang ZK Davies KP Kalpana GV January 2002 A masked NES in INI1 hSNF5 mediates hCRM1 dependent nuclear export implications for tumorigenesis EMBO J 21 1 2 31 42 doi 10 1093 emboj 21 1 31 PMC 125819 PMID 11782423 Kanai M Hanashiro K Kim SH Hanai S Boulares AH Miwa M Fukasawa K September 2007 Inhibition of Crm1 p53 interaction and nuclear export of p53 by poly ADP ribosyl ation Nat Cell Biol 9 10 1175 83 doi 10 1038 ncb1638 PMID 17891139 S2CID 13433567 Shao C Lu C Chen L Koty PP Cobos E Gao W August 2010 p53 Dependent anticancer effects of leptomycin B on lung adenocarcinoma Cancer Chemother Pharmacol 67 6 1369 80 doi 10 1007 s00280 010 1434 6 PMID 20803015 S2CID 27127578 Further reading editGorlich D Kutay U 1999 Transport between the cell nucleus and the cytoplasm Annu Rev Cell Dev Biol 15 1 607 60 doi 10 1146 annurev cellbio 15 1 607 PMID 10611974 Budhu AS Wang XW 2007 Loading and unloading orchestrating centrosome duplication and spindle assembly by Ran Crm1 Cell Cycle 4 11 1510 4 doi 10 4161 cc 4 11 2187 PMC 1402358 PMID 16294017 Li L Li HS Pauza CD Bukrinsky M Zhao RY 2006 Roles of HIV 1 auxiliary proteins in viral pathogenesis and host pathogen interactions Cell Res 15 11 12 923 34 doi 10 1038 sj cr 7290370 PMID 16354571 Stauber RH Mann W Knauer SK 2007 Nuclear and cytoplasmic survivin molecular mechanism prognostic and therapeutic potential Cancer Res 67 13 5999 6002 doi 10 1158 0008 5472 CAN 07 0494 PMID 17616652 Mathew C Ghildyal R 2017 CRM1 inhibitors for antiviral therapy Frontiers in Microbiology 8 1171 doi 10 3389 fmicb 2017 01171 PMC 5487384 PMID 28702009 External links edit3D electron microscopy structures of CRM1 from the EM Data Bank EMDB nbsp This article on a gene on human chromosome 2 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title XPO1 amp oldid 1187008070, wikipedia, wiki, book, books, library,

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