Exportin 1 (CRM1 homolog, yeast)

PDB rendering based on 1w9c.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols XPO1; CRM1; emb; exp1
External IDs OMIM: 602559 MGI: 2144013 HomoloGene: 2554 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_003400.3 NM_001035226.1
RefSeq (protein) NP_003391.1 NP_001030303.1
Location (UCSC) Chr 2:
61.7 – 61.77 Mb		 Chr 11:
23.16 – 23.2 Mb
PubMed search [1] [2]
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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]

Contents

Interactions [link]

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] p53, [15][16] and CDKN1B.[17][18]

See also [link]

References [link]

  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, 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)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7514. 
  4. ^ Thomas, Franziska; Kutay Ulrike (June 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 (January 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 (April 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. //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 (June 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. //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 (August 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133185. 
  10. ^ a b Tickenbrock, Lara; Cramer Janina, Vetter Ingrid R, Muller Oliver (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. (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 (September 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. //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 (January 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125819. 
  15. ^ Kanai, Masayuki; Kazuhiko Hanashiro, Song-Hee Kim, Shuji Hanai, A. Hamid Boulares, Masanao Miwa, Kenji Fukasawa V (September 2007). "Inhibition of Crm1–p53 interaction and nuclear export of p53 by poly(ADP-ribosyl)ation". Nature Cell Biology (United States) 9: 1175 - 1183. DOI:10.1038/ncb1638. ISSN 1465-7392. PMID 17891139. 
  16. ^ Shao, Changxia; Chuanwen Lu, Lixia Chen, Patrick P. Koty, Everardo Cobos and Weimin Gao V (August 2010). "p53-dependent anticancer effects of leptomycin B on lung adenocarcinoma". Cancer Chemotherapy and Pharmacology (United States) 67 (6): 1369-1380. DOI:10.1007/s00280-010-1434-6. ISSN 0344-5704. PMID 20803015. 
  17. ^ Ishida, Noriko; Hara Taichi, Kamura Takumi, Yoshida Minoru, Nakayama Keiko, Nakayama Keiichi I (April 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. 
  18. ^ Connor, Michael K; Kotchetkov Rouslan, Cariou Sandrine, Resch Ansgar, Lupetti Rafaella, Beniston Richard G, Melchior Frauke, Hengst Ludger, Slingerland Joyce M (January 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. //www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=140238. 

Further reading [link]



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