XPO1

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Exportin 1
Exportin1, CRM1, free form.jpg
PDB rendering based on 4FGV.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols XPO1 ; CRM1; emb; exp1
External IDs OMIM602559 MGI2144013 HomoloGene2554 ChEMBL: 5661 GeneCards: XPO1 Gene
RNA expression pattern
PBB GE XPO1 208775 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 7514 103573
Ensembl ENSG00000082898 ENSMUSG00000020290
UniProt O14980 Q6P5F9
RefSeq (mRNA) NM_003400 NM_001035226
RefSeq (protein) NP_003391 NP_001030303
Location (UCSC) Chr 2:
61.7 – 61.77 Mb
Chr 11:
23.26 – 23.3 Mb
PubMed search [1] [2]

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

Function[edit]

Exportin 1 mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically inhibits 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, MPAK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1.[4]

Interactions[edit]

XPO1 has been shown to interact with:

See also[edit]

References[edit]

  1. ^ Fornerod M, van Baal S, Valentine V, Shapiro DN, Grosveld G (September 1997). "Chromosomal localization of genes encoding CAN/Nup214-interacting proteins--human CRM1 localizes to 2p16, whereas Nup88 localizes to 17p13 and is physically linked to SF2p32". Genomics 42 (3): 538–40. doi:10.1006/geno.1997.4767. PMID 9205132. 
  2. ^ Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M et al. (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. 
  4. ^ "Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)". 
  5. ^ 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. 
  6. ^ 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. 
  7. ^ Connor MK, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston RG et al. (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. 
  8. ^ 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. 
  9. ^ 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. 
  10. ^ 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. 
  11. ^ 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. 
  12. ^ 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. 
  13. ^ 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. 
  14. ^ 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. 
  15. ^ 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. 
  16. ^ 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. 
  17. ^ 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. 
  18. ^ Kanai M, Hanashiro K, Kim SH, Hanai S, Boulares AH, Miwa M et al. (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. 
  19. ^ 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[edit]

External links[edit]