XPO1

XPO1
Available structures
PDB	Ortholog search: C9JV99 PDBe C9JV99 RCSB
List of PDB id codes
	1W9C, 2L1L, 3GB8, 4BSM, 4BSN, 5DIS
Identifiers
Aliases	XPO1, CRM1, emb, exp1, exportin 1, CRM-1
External IDs	OMIM: 602559; MGI: 2144013; HomoloGene: 2554; GeneCards: XPO1; OMA:XPO1 - orthologs
Gene location (Human)
Chr.	Chromosome 2 (human)
End	61,538,741 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	23,248,249 bp
RNA expression pattern
	Top expressed in
	tibia; ; germinal epithelium; ; parietal pleura; ; visceral pleura; ; embryo; ; trabecular bone; ; palpebral conjunctiva; ; ganglionic eminence; ; retinal pigment epithelium; ; superficial temporal artery;
	Top expressed in
	primitive streak; ; dermis; ; abdominal wall; ; medullary collecting duct; ; maxillary prominence; ; renal corpuscle; ; somite; ; cumulus cell; ; medial ganglionic eminence; ; vas deferens;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein domain specific binding; transporter activity; protein binding; RNA binding; structural constituent of nuclear pore; nuclear export signal receptor activity;
Cellular component	cytoplasm; 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 structure;
Biological process	ribosomal 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 transport;
	Sources:Amigo / QuickGO
Orthologs
	7514
	103573
	ENSG00000082898
	ENSMUSG00000020290
	O14980
	Q6P5F9
	NM_003400
	NM_001035226; NM_134014
	NP_003391
	NP_001030303; NP_598775
	Wikidata
View/Edit Human	View/Edit Mouse

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.^[5]^[6]^[7]^[8]

Function

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.^[9]

Interactions

XPO1 has been shown to interact with:

References

^ ^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.
^ 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.
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.
^ 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.
^ "Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)".
^ ^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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)
^ 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.
^ 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.
^ 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.
^ 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.

External links

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

This article on a gene on human chromosome 2 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000082898 – Ensembl, May 2017

[refGRCm38Ensembl-2] 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.

[pmid9205132-5] 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.

[pmid9368044-6] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[7] 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.

[8] 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.

[9] "Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)".

[pmid12070164-10] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid11889117-11] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid12529437-12] 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.

[pmid12517958-13] 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.

[pmid18245089-14] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid12724356-15] 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.

[pmid11425870-16] 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.

[pmid10330396-17] 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.

[pmid10779340-18] 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.

[pmid10601307-19] 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.{{cite journal}}: CS1 maint: unflagged free DOI (link)

[pmid12176322-20] 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.

[pmid9323133-21] 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.

[pmid11782423-22] 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.

[23] 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.

[pmid20803015-24] 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.

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

XPO1

Function

Interactions

See also

References

Further reading

External links