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XPO1

Introduction

Exportin 1 (XPO1), also known as chromosomal maintenance 1 (CRM1), is an eukaryotic protein that mediates the nuclear export of proteins, rRNA, snRNA, and some mRNA.[1][2][3][4]

History

History

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]

Function

Function

Exportin 1 mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically mediates the nuclear export of Rev and U snRNAs. It is involved in the control of several cellular processes by controlling the localization of cyclin B, MAPK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1.[6]

Interactions

Interactions

XPO1 has been shown to interact with:

See also

See also

References

References

  1. ↑ 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.
  2. ↑ Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M, Horinouchi S (Dec 1997). “Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins”. J Biol Chem. 272 (47): 29742–51. doi:10.1074/jbc.272.47.29742. PMID 9368044.
  3. ↑ 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. PMID 17786152.
  4. ↑ Lu C, Figueroa JA, Liu Z, Konala V, Aulakh A, Verma R, Cobos E, Chiriva-Internati M, Gao W (September 2015). “Nuclear Export as a Novel Therapeutic Target: The CRM1 Connection”. Current Cancer Drug Targets. 15 (7): 575–592. doi:10.2174/156800961507150828223554.
  5. ↑ Noske A, Weichert W, Niesporek S, Röske A, Buckendahl AC, Koch I, Sehouli J, Dietel M, Denkert C (Apr 2008). “Expression of the nuclear export protein chromosomal region maintenance/exportin 1/Xpo1 is a prognostic factor in human ovarian cancer”. Cancer. 112 (8): 1733–43. doi:10.1002/cncr.23354. PMID 18306389.
  6. ↑ “Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)”.
  7. ↑ 7.0 7.1 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.
  8. ↑ 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.
  9. ↑ 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.
  10. ↑ 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.
  11. ↑ 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.
  12. ↑ 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.
  13. ↑ 13.0 13.1 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.
  14. ↑ 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.
  15. ↑ 15.0 15.1 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.
  16. ↑ 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.
  17. ↑ 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.
  18. ↑ 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.
  19. ↑ 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.
  20. ↑ 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.
  21. ↑ 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.
Further reading

Further reading

External links