β-Catenin can bind directly to CRM1 independently of adenomatous polyposis coli, which affects its nuclear localization and LEF-1/β-catenin-dependent gene expression
Nuclear β-catenin affects the developmental process and progression of tumors. However, the precise mechanism for the nuclear export of β-catenin is not completely understood. We found that β-catenin can bind directly to CRM1 through its central armadillo (ARM) repeats region, independently of the a...
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| Veröffentlicht in: | Cell biology international 2008-04, Vol.32 (4), p.394-400 |
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| description | Nuclear β-catenin affects the developmental process and progression of tumors. However, the precise mechanism for the nuclear export of β-catenin is not completely understood. We found that β-catenin can bind directly to CRM1 through its central armadillo (ARM) repeats region, independently of the adenomatous polyposis coli (APC) protein. CRM1 overexpression transports nuclear β-catenin into the cytoplasm and decreases LEF-1/β-catenin-dependent transcriptional activity, which is also affected by the co-overexpression of E-cadherin. CRM1 competed with E-cadherin and LEF-1 for binding to β-catenin. β-catenin could interact directly with APC through its essential sequences between amino acids 342 and 350. The site-directed β-catenin mutant (NES2
−), which could interact with CRM1, but not with APC, still retained its ability to export from the nucleus and its transactivational activity. This suggests that CRM1 can function as an efficient nuclear exporter for β-catenin independently of APC. These results strongly suggest that the CRM1-mediated pathway is involved in the efficient transport of nuclear β-catenin in the nucleus of cells. |
| doi_str_mv | 10.1016/j.cellbi.2007.12.008 |
| format | Article |
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−), which could interact with CRM1, but not with APC, still retained its ability to export from the nucleus and its transactivational activity. This suggests that CRM1 can function as an efficient nuclear exporter for β-catenin independently of APC. These results strongly suggest that the CRM1-mediated pathway is involved in the efficient transport of nuclear β-catenin in the nucleus of cells.</description><identifier>ISSN: 1065-6995</identifier><identifier>EISSN: 1095-8355</identifier><identifier>DOI: 10.1016/j.cellbi.2007.12.008</identifier><identifier>PMID: 18262809</identifier><language>eng</language><publisher>Oxford, UK: Elsevier Ltd</publisher><subject>Active Transport, Cell Nucleus ; Adenomatous polyposis coli ; Adenomatous Polyposis Coli Protein - metabolism ; Amino Acid Sequence ; Animals ; beta Catenin - chemistry ; beta Catenin - metabolism ; Binding, Competitive ; Cadherins - metabolism ; Cell Nucleus - metabolism ; CRM1 ; Exportin 1 Protein ; Gene Expression Regulation ; Karyopherins - metabolism ; LEF-1 ; Lymphoid Enhancer-Binding Factor 1 - metabolism ; Mice ; Models, Biological ; Molecular Sequence Data ; NIH 3T3 Cells ; Nuclear export ; Nuclear Export Signals ; Protein Binding ; Receptors, Cytoplasmic and Nuclear - metabolism ; Repetitive Sequences, Amino Acid ; β-Catenin</subject><ispartof>Cell biology international, 2008-04, Vol.32 (4), p.394-400</ispartof><rights>2008 International Federation for Cell Biology</rights><rights>The Author(s) Journal compilation © 2008 International Federation for Cell Biology</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4494-732b91c3635715e3dc897b0a9f6f030dd005a5308de45c05843e592c039e24503</citedby><cites>FETCH-LOGICAL-c4494-732b91c3635715e3dc897b0a9f6f030dd005a5308de45c05843e592c039e24503</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.cellbi.2007.12.008$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2Fj.cellbi.2007.12.008$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,778,782,1414,27907,27908,45557,45558</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18262809$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ki, Hyunkyoung</creatorcontrib><creatorcontrib>Oh, Minsoo</creatorcontrib><creatorcontrib>Chung, Su Wol</creatorcontrib><creatorcontrib>Kim, Kwonseop</creatorcontrib><title>β-Catenin can bind directly to CRM1 independently of adenomatous polyposis coli, which affects its nuclear localization and LEF-1/β-catenin-dependent gene expression</title><title>Cell biology international</title><addtitle>Cell Biol Int</addtitle><description>Nuclear β-catenin affects the developmental process and progression of tumors. However, the precise mechanism for the nuclear export of β-catenin is not completely understood. We found that β-catenin can bind directly to CRM1 through its central armadillo (ARM) repeats region, independently of the adenomatous polyposis coli (APC) protein. CRM1 overexpression transports nuclear β-catenin into the cytoplasm and decreases LEF-1/β-catenin-dependent transcriptional activity, which is also affected by the co-overexpression of E-cadherin. CRM1 competed with E-cadherin and LEF-1 for binding to β-catenin. β-catenin could interact directly with APC through its essential sequences between amino acids 342 and 350. The site-directed β-catenin mutant (NES2
−), which could interact with CRM1, but not with APC, still retained its ability to export from the nucleus and its transactivational activity. This suggests that CRM1 can function as an efficient nuclear exporter for β-catenin independently of APC. These results strongly suggest that the CRM1-mediated pathway is involved in the efficient transport of nuclear β-catenin in the nucleus of cells.</description><subject>Active Transport, Cell Nucleus</subject><subject>Adenomatous polyposis coli</subject><subject>Adenomatous Polyposis Coli Protein - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>beta Catenin - chemistry</subject><subject>beta Catenin - metabolism</subject><subject>Binding, Competitive</subject><subject>Cadherins - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>CRM1</subject><subject>Exportin 1 Protein</subject><subject>Gene Expression Regulation</subject><subject>Karyopherins - metabolism</subject><subject>LEF-1</subject><subject>Lymphoid Enhancer-Binding Factor 1 - metabolism</subject><subject>Mice</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>NIH 3T3 Cells</subject><subject>Nuclear export</subject><subject>Nuclear Export Signals</subject><subject>Protein Binding</subject><subject>Receptors, Cytoplasmic and Nuclear - metabolism</subject><subject>Repetitive Sequences, Amino Acid</subject><subject>β-Catenin</subject><issn>1065-6995</issn><issn>1095-8355</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUstu1DAUjRCIlsIfIOQVK5La8SM2C6ROaEuloUg8xNLyODfUQ8YOcabt9IfY8yF8E44yKjvEwvbV1TnnPo6z7DnBBcFEHK8LC123ckWJcVWQssBYPsgOCVY8l5Tzh1MseC6U4gfZkxjXGBPCpHicHRBZilJidZj9_P0rr80I3nlkjUcr5xvUuAHs2O3QGFD98T1BKQk9pMtP2dAik8KwMWPYRtSHbteH6CKyoXOv0M2Vs1fItG3SiMil47e2AzOgLljTuTszuuCRSYWWp2c5OU4t2LmF_L4M-gYeENz2A8SY4E-zR63pIjzbv0fZl7PTz_W7fPnh_KI-WeaWMcXyipYrRSwVlFeEA22sVNUKG9WKFlPcNBhzwymWDTBuMZeMAlelxVRByTimR9nLWbcfwo8txFFvXJwWbTykYbVQRFBRsQRkM9AOIcYBWt0PbmOGnSZYTwbptZ4N0pNBmpQ6GZRoL_b629UGmr-kvSMJ8HoG3LgOdv8lquvFxWUp1dRUPpNdHOH2nmyG71pUtOL66-W5fks_VXKxYHqa9s2Mh7TSaweDjtaBtzD_AN0E9-9x_gBcVMd7</recordid><startdate>200804</startdate><enddate>200804</enddate><creator>Ki, Hyunkyoung</creator><creator>Oh, Minsoo</creator><creator>Chung, Su Wol</creator><creator>Kim, Kwonseop</creator><general>Elsevier Ltd</general><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>200804</creationdate><title>β-Catenin can bind directly to CRM1 independently of adenomatous polyposis coli, which affects its nuclear localization and LEF-1/β-catenin-dependent gene expression</title><author>Ki, Hyunkyoung ; Oh, Minsoo ; Chung, Su Wol ; Kim, Kwonseop</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4494-732b91c3635715e3dc897b0a9f6f030dd005a5308de45c05843e592c039e24503</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Active Transport, Cell Nucleus</topic><topic>Adenomatous polyposis coli</topic><topic>Adenomatous Polyposis Coli Protein - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>beta Catenin - chemistry</topic><topic>beta Catenin - metabolism</topic><topic>Binding, Competitive</topic><topic>Cadherins - metabolism</topic><topic>Cell Nucleus - metabolism</topic><topic>CRM1</topic><topic>Exportin 1 Protein</topic><topic>Gene Expression Regulation</topic><topic>Karyopherins - metabolism</topic><topic>LEF-1</topic><topic>Lymphoid Enhancer-Binding Factor 1 - metabolism</topic><topic>Mice</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>NIH 3T3 Cells</topic><topic>Nuclear export</topic><topic>Nuclear Export Signals</topic><topic>Protein Binding</topic><topic>Receptors, Cytoplasmic and Nuclear - metabolism</topic><topic>Repetitive Sequences, Amino Acid</topic><topic>β-Catenin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ki, Hyunkyoung</creatorcontrib><creatorcontrib>Oh, Minsoo</creatorcontrib><creatorcontrib>Chung, Su Wol</creatorcontrib><creatorcontrib>Kim, Kwonseop</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell biology international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ki, Hyunkyoung</au><au>Oh, Minsoo</au><au>Chung, Su Wol</au><au>Kim, Kwonseop</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>β-Catenin can bind directly to CRM1 independently of adenomatous polyposis coli, which affects its nuclear localization and LEF-1/β-catenin-dependent gene expression</atitle><jtitle>Cell biology international</jtitle><addtitle>Cell Biol Int</addtitle><date>2008-04</date><risdate>2008</risdate><volume>32</volume><issue>4</issue><spage>394</spage><epage>400</epage><pages>394-400</pages><issn>1065-6995</issn><eissn>1095-8355</eissn><abstract>Nuclear β-catenin affects the developmental process and progression of tumors. However, the precise mechanism for the nuclear export of β-catenin is not completely understood. We found that β-catenin can bind directly to CRM1 through its central armadillo (ARM) repeats region, independently of the adenomatous polyposis coli (APC) protein. CRM1 overexpression transports nuclear β-catenin into the cytoplasm and decreases LEF-1/β-catenin-dependent transcriptional activity, which is also affected by the co-overexpression of E-cadherin. CRM1 competed with E-cadherin and LEF-1 for binding to β-catenin. β-catenin could interact directly with APC through its essential sequences between amino acids 342 and 350. The site-directed β-catenin mutant (NES2
−), which could interact with CRM1, but not with APC, still retained its ability to export from the nucleus and its transactivational activity. This suggests that CRM1 can function as an efficient nuclear exporter for β-catenin independently of APC. These results strongly suggest that the CRM1-mediated pathway is involved in the efficient transport of nuclear β-catenin in the nucleus of cells.</abstract><cop>Oxford, UK</cop><pub>Elsevier Ltd</pub><pmid>18262809</pmid><doi>10.1016/j.cellbi.2007.12.008</doi><tpages>7</tpages></addata></record> |
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| subjects | Active Transport, Cell Nucleus Adenomatous polyposis coli Adenomatous Polyposis Coli Protein - metabolism Amino Acid Sequence Animals beta Catenin - chemistry beta Catenin - metabolism Binding, Competitive Cadherins - metabolism Cell Nucleus - metabolism CRM1 Exportin 1 Protein Gene Expression Regulation Karyopherins - metabolism LEF-1 Lymphoid Enhancer-Binding Factor 1 - metabolism Mice Models, Biological Molecular Sequence Data NIH 3T3 Cells Nuclear export Nuclear Export Signals Protein Binding Receptors, Cytoplasmic and Nuclear - metabolism Repetitive Sequences, Amino Acid β-Catenin |
| title | β-Catenin can bind directly to CRM1 independently of adenomatous polyposis coli, which affects its nuclear localization and LEF-1/β-catenin-dependent gene expression |
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