XPO1

Exportin 1 (CRM1 homolog, yeast)
PDB rendering based on 1w9c.
Available structures PDB 1W9C, 3GB8
Identifiers
Symbols	XPO1; CRM1; DKFZp686B1823; emb
External IDs	OMIM: 602559 MGI: 2144013 HomoloGene: 2554 GeneCards: XPO1 Gene
Gene Ontology Molecular function • RNA binding • protein binding • protein transporter activity Cellular component • kinetochore • nucleus • nuclear envelope • annulate lamellae • nucleoplasm • nucleoplasm • nucleolus • cytoplasm • cytosol • cytosol • Cajal body • ribonucleoprotein complex Biological process • M phase of mitotic cell cycle • mitotic prometaphase • mitotic cell cycle • intracellular protein transport • viral reproduction • RNA metabolic process • mRNA metabolic process • viral infectious cycle • interspecies interaction between organisms • viral genome transport in host cell • mRNA transport Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7514	103573
Ensembl	ENSG00000082898	ENSMUSG00000020290
UniProt	O14980	Q8BYY5
RefSeq (mRNA)	NM_003400.3	NM_001035226
RefSeq (protein)	NP_003391.1	NP_001030303
Location (UCSC)	Chr 2: 61.7 – 61.77 Mb	Chr 11: 23.16 – 23.2 Mb
PubMed search	[1]	[2]

Exportin-1 is a protein that in humans is encoded by the XPO1 gene.^[1][2]

The protein encoded by this gene 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.^[3]

Interactions

XPO1 has been shown to interact with NMD3,^[4] CIITA,^[5][6] RANBP3,^[7][8] Nucleoporin 62,^[7][9] Ran,^[10][11][12] RANBP1,^[12][13] APC,^[10] SMARCB1^[14] and CDKN1B.^[15][16]

See also

• Karyopherin

References

1. ^ Fornerod M, van Baal S, Valentine V, Shapiro DN, Grosveld G (Sep 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, 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. ^ "Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7514. 
4. ^ Thomas, Franziska; Kutay Ulrike (Jun. 2003). "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway". J. Cell. Sci. (England) 116 (Pt 12): 2409–19. doi:10.1242/jcs.00464. ISSN 0021-9533. PMID 12724356. 
5. ^ Raval, Aparna; Weissman Jocelyn D, Howcroft T Kevin, Singer Dinah S (Jan. 2003). "The GTP-binding domain of class II transactivator regulates its nuclear export". J. Immunol. (United States) 170 (2): 922–30. ISSN 0022-1767. PMID 12517958. 
6. ^ Voong, Lilien N; Slater Allison R, Kratovac Sebila, Cressman Drew E (Apr. 2008). "Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator". J. Biol. Chem. (United States) 283 (14): 9031–9. doi:10.1074/jbc.M706487200. ISSN 0021-9258. PMC 2431044. PMID 18245089. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2431044. 
7. ^ ^{a b} Lindsay, M E; Holaska J M, Welch K, Paschal B M, Macara I G (Jun. 2001). "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export". J. Cell Biol. (United States) 153 (7): 1391–402. doi:10.1083/jcb.153.7.1391. ISSN 0021-9525. PMC 2150735. PMID 11425870. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2150735. 
8. ^ Lindsay, Mark E; Plafker Kendra, Smith Alicia E, Clurman Bruce E, Macara Ian G (Aug. 2002). "Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import". Cell (United States) 110 (3): 349–60. doi:10.1016/S0092-8674(02)00836-X. ISSN 0092-8674. PMID 12176322. 
9. ^ Kehlenbach, R H; 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. (UNITED STATES) 145 (4): 645–57. doi:10.1083/jcb.145.4.645. ISSN 0021-9525. PMC 2133185. PMID 10330396. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133185. 
10. ^ ^{a b} Tickenbrock, Lara; Cramer Janina, Vetter Ingrid R, Muller Oliver (Aug. 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. (United States) 277 (35): 32332–8. doi:10.1074/jbc.M203990200. ISSN 0021-9258. PMID 12070164. 
11. ^ Fornerod, M; Ohno M, Yoshida M, Mattaj I W (Sep. 1997). "CRM1 is an export receptor for leucine-rich nuclear export signals". Cell (UNITED STATES) 90 (6): 1051–60. doi:10.1016/S0092-8674(00)80371-2. ISSN 0092-8674. PMID 9323133. 
12. ^ ^{a b} Plafker, K; Macara I G (May. 2000). "Facilitated nucleocytoplasmic shuttling of the Ran binding protein RanBP1". Mol. Cell. Biol. (UNITED STATES) 20 (10): 3510–21. doi:10.1128/MCB.20.10.3510-3521.2000. ISSN 0270-7306. PMC 85643. PMID 10779340. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=85643. 
13. ^ Singh, B B; Patel H H, Roepman R, Schick D, Ferreira P A (Dec. 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem. (UNITED STATES) 274 (52): 37370–8. doi:10.1074/jbc.274.52.37370. ISSN 0021-9258. PMID 10601307. 
14. ^ Craig, Errol; Zhang Zhi-Kai, Davies Kelvin P, Kalpana Ganjam V (Jan. 2002). "A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis". EMBO J. (England) 21 (1-2): 31–42. doi:10.1093/emboj/21.1.31. ISSN 0261-4189. PMC 125819. PMID 11782423. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125819. 
15. ^ Ishida, Noriko; Hara Taichi, Kamura Takumi, Yoshida Minoru, Nakayama Keiko, Nakayama Keiichi I (Apr. 2002). "Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export". J. Biol. Chem. (United States) 277 (17): 14355–8. doi:10.1074/jbc.C100762200. ISSN 0021-9258. PMID 11889117. 
16. ^ Connor, Michael K; Kotchetkov Rouslan, Cariou Sandrine, Resch Ansgar, Lupetti Rafaella, Beniston Richard G, Melchior Frauke, Hengst Ludger, Slingerland Joyce M (Jan. 2003). "CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis". Mol. Biol. Cell (United States) 14 (1): 201–13. doi:10.1091/mbc.E02-06-0319. ISSN 1059-1524. PMC 140238. PMID 12529437. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140238. 

Further reading

• 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. PMC 1402358. PMID 16294017. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1402358. 
• Li L, Li HS, Pauza CD, et al. (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.