Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA
Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm and binds specifica...
Gespeichert in:
| Veröffentlicht in: | Scientific reports 2011-09, Vol.1 (1), p.92-92, Article 92 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 92 |
|---|---|
| container_issue | 1 |
| container_start_page | 92 |
| container_title | Scientific reports |
| container_volume | 1 |
| creator | Kataoka, Naoyuki Diem, Michael D. Yoshida, Mayumi Hatai, Chihiro Dobashi, Izumi Dreyfuss, Gideon Hagiwara, Masatoshi Ohno, Mutsuhito |
| description | Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14’s carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh. |
| doi_str_mv | 10.1038/srep00092 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3216578</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1897393402</sourcerecordid><originalsourceid>FETCH-LOGICAL-c437t-61b508b5fcd8f2b11d51f236d7b216441b6ecb75b4f42ceacb731fe009ace7103</originalsourceid><addsrcrecordid>eNplkVtLHEEQhZsQiYv64B8IDXkIBkb7OpeXgCxGA6Lg5cGnpqenZ7eXme7JdE9k_70lq8uaPFVBfZw6VQehY0pOKeHlWRztQAip2Cc0Y0TIjHHGPu_0--goxhUgRLJK0OoL2meMS5lTMkPqfrDGtc7gJypwE3rtfMS9bZxOFrsUsZ9MZ0Nm1ikMnY49oHE5pdQ5v8DaN1jHGAzgLnj87NISx6Fzxja4v7s5P0R7re6iPXqrB-jx18XD_Cq7vr38PT-_zozgRcpyWktS1rI1TdmymtJG0pbxvClqRnMhaJ1bUxeyFq1gxmroOW0tnK2NLeAPB-jnRneYanBvrE-j7tQwul6PaxW0Ux8n3i3VIvxVHPRlUYLA9zeBMfyZbEyqd9HYrtPehimqinFacZHnQH77h1yFafRwnaJlVXCgCAPqZEOZMUTIqN16oUS9Bqe2wQH7ddf8lnyPCYAfGyDCyC_suLPyP7UXmUGjKw</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1897393402</pqid></control><display><type>article</type><title>Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA</title><source>MEDLINE</source><source>DOAJ Directory of Open Access Journals</source><source>EZB-FREE-00999 freely available EZB journals</source><source>PubMed Central</source><source>Free Full-Text Journals in Chemistry</source><creator>Kataoka, Naoyuki ; Diem, Michael D. ; Yoshida, Mayumi ; Hatai, Chihiro ; Dobashi, Izumi ; Dreyfuss, Gideon ; Hagiwara, Masatoshi ; Ohno, Mutsuhito</creator><creatorcontrib>Kataoka, Naoyuki ; Diem, Michael D. ; Yoshida, Mayumi ; Hatai, Chihiro ; Dobashi, Izumi ; Dreyfuss, Gideon ; Hagiwara, Masatoshi ; Ohno, Mutsuhito</creatorcontrib><description>Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14’s carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep00092</identifier><identifier>PMID: 22355610</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/1647 ; 631/326 ; 631/45 ; 631/80 ; Amino Acid Sequence ; Biochemistry ; Biology ; Cell Nucleus - metabolism ; Cytoplasm ; Cytoplasm - metabolism ; Exons ; Gene expression ; HeLa Cells ; Humanities and Social Sciences ; Humans ; Insects ; Kinases ; Localization ; Molecular Sequence Data ; Monoclonal antibodies ; mRNA ; multidisciplinary ; Nuclear Export Signals ; Nuclear transport ; Peptides ; Protein Transport ; Proteins ; RNA Splicing ; RNA, Messenger - metabolism ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - metabolism ; Science ; Splicing</subject><ispartof>Scientific reports, 2011-09, Vol.1 (1), p.92-92, Article 92</ispartof><rights>The Author(s) 2011</rights><rights>Copyright Nature Publishing Group Sep 2011</rights><rights>Copyright © 2011, Macmillan Publishers Limited. All rights reserved 2011 Macmillan Publishers Limited. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-61b508b5fcd8f2b11d51f236d7b216441b6ecb75b4f42ceacb731fe009ace7103</citedby><cites>FETCH-LOGICAL-c437t-61b508b5fcd8f2b11d51f236d7b216441b6ecb75b4f42ceacb731fe009ace7103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3216578/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3216578/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22355610$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kataoka, Naoyuki</creatorcontrib><creatorcontrib>Diem, Michael D.</creatorcontrib><creatorcontrib>Yoshida, Mayumi</creatorcontrib><creatorcontrib>Hatai, Chihiro</creatorcontrib><creatorcontrib>Dobashi, Izumi</creatorcontrib><creatorcontrib>Dreyfuss, Gideon</creatorcontrib><creatorcontrib>Hagiwara, Masatoshi</creatorcontrib><creatorcontrib>Ohno, Mutsuhito</creatorcontrib><title>Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14’s carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh.</description><subject>631/1647</subject><subject>631/326</subject><subject>631/45</subject><subject>631/80</subject><subject>Amino Acid Sequence</subject><subject>Biochemistry</subject><subject>Biology</subject><subject>Cell Nucleus - metabolism</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Exons</subject><subject>Gene expression</subject><subject>HeLa Cells</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>Insects</subject><subject>Kinases</subject><subject>Localization</subject><subject>Molecular Sequence Data</subject><subject>Monoclonal antibodies</subject><subject>mRNA</subject><subject>multidisciplinary</subject><subject>Nuclear Export Signals</subject><subject>Nuclear transport</subject><subject>Peptides</subject><subject>Protein Transport</subject><subject>Proteins</subject><subject>RNA Splicing</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Science</subject><subject>Splicing</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNplkVtLHEEQhZsQiYv64B8IDXkIBkb7OpeXgCxGA6Lg5cGnpqenZ7eXme7JdE9k_70lq8uaPFVBfZw6VQehY0pOKeHlWRztQAip2Cc0Y0TIjHHGPu_0--goxhUgRLJK0OoL2meMS5lTMkPqfrDGtc7gJypwE3rtfMS9bZxOFrsUsZ9MZ0Nm1ikMnY49oHE5pdQ5v8DaN1jHGAzgLnj87NISx6Fzxja4v7s5P0R7re6iPXqrB-jx18XD_Cq7vr38PT-_zozgRcpyWktS1rI1TdmymtJG0pbxvClqRnMhaJ1bUxeyFq1gxmroOW0tnK2NLeAPB-jnRneYanBvrE-j7tQwul6PaxW0Ux8n3i3VIvxVHPRlUYLA9zeBMfyZbEyqd9HYrtPehimqinFacZHnQH77h1yFafRwnaJlVXCgCAPqZEOZMUTIqN16oUS9Bqe2wQH7ddf8lnyPCYAfGyDCyC_suLPyP7UXmUGjKw</recordid><startdate>20110914</startdate><enddate>20110914</enddate><creator>Kataoka, Naoyuki</creator><creator>Diem, Michael D.</creator><creator>Yoshida, Mayumi</creator><creator>Hatai, Chihiro</creator><creator>Dobashi, Izumi</creator><creator>Dreyfuss, Gideon</creator><creator>Hagiwara, Masatoshi</creator><creator>Ohno, Mutsuhito</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20110914</creationdate><title>Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA</title><author>Kataoka, Naoyuki ; Diem, Michael D. ; Yoshida, Mayumi ; Hatai, Chihiro ; Dobashi, Izumi ; Dreyfuss, Gideon ; Hagiwara, Masatoshi ; Ohno, Mutsuhito</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-61b508b5fcd8f2b11d51f236d7b216441b6ecb75b4f42ceacb731fe009ace7103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>631/1647</topic><topic>631/326</topic><topic>631/45</topic><topic>631/80</topic><topic>Amino Acid Sequence</topic><topic>Biochemistry</topic><topic>Biology</topic><topic>Cell Nucleus - metabolism</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>Exons</topic><topic>Gene expression</topic><topic>HeLa Cells</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Insects</topic><topic>Kinases</topic><topic>Localization</topic><topic>Molecular Sequence Data</topic><topic>Monoclonal antibodies</topic><topic>mRNA</topic><topic>multidisciplinary</topic><topic>Nuclear Export Signals</topic><topic>Nuclear transport</topic><topic>Peptides</topic><topic>Protein Transport</topic><topic>Proteins</topic><topic>RNA Splicing</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Science</topic><topic>Splicing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kataoka, Naoyuki</creatorcontrib><creatorcontrib>Diem, Michael D.</creatorcontrib><creatorcontrib>Yoshida, Mayumi</creatorcontrib><creatorcontrib>Hatai, Chihiro</creatorcontrib><creatorcontrib>Dobashi, Izumi</creatorcontrib><creatorcontrib>Dreyfuss, Gideon</creatorcontrib><creatorcontrib>Hagiwara, Masatoshi</creatorcontrib><creatorcontrib>Ohno, Mutsuhito</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kataoka, Naoyuki</au><au>Diem, Michael D.</au><au>Yoshida, Mayumi</au><au>Hatai, Chihiro</au><au>Dobashi, Izumi</au><au>Dreyfuss, Gideon</au><au>Hagiwara, Masatoshi</au><au>Ohno, Mutsuhito</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2011-09-14</date><risdate>2011</risdate><volume>1</volume><issue>1</issue><spage>92</spage><epage>92</epage><pages>92-92</pages><artnum>92</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Pre-mRNA splicing deposits multi-protein complexes, termed exon junction complexes (EJCs), on mRNAs near exon-exon junctions. The core of EJC consists of four proteins, eIF4AIII, MLN51, Y14 and Magoh. Y14 is a nuclear protein that can shuttle between the nucleus and the cytoplasm and binds specifically to Magoh. Here we delineate a Y14 nuclear localization signal that also confers its nuclear export, which we name YNS. We further identified a 12-amino-acid peptide near Y14’s carboxyl terminus that is required for its association with spliced mRNAs, as well as for Magoh binding. Furthermore, the Y14 mutants, which are deficient in binding to Magoh, could still be localized to the nucleus, suggesting the existence of both the nuclear import pathway and function for Y14 unaccompanied by Magoh.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>22355610</pmid><doi>10.1038/srep00092</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-2322 |
| ispartof | Scientific reports, 2011-09, Vol.1 (1), p.92-92, Article 92 |
| issn | 2045-2322 2045-2322 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3216578 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | 631/1647 631/326 631/45 631/80 Amino Acid Sequence Biochemistry Biology Cell Nucleus - metabolism Cytoplasm Cytoplasm - metabolism Exons Gene expression HeLa Cells Humanities and Social Sciences Humans Insects Kinases Localization Molecular Sequence Data Monoclonal antibodies mRNA multidisciplinary Nuclear Export Signals Nuclear transport Peptides Protein Transport Proteins RNA Splicing RNA, Messenger - metabolism RNA-Binding Proteins - chemistry RNA-Binding Proteins - metabolism Science Splicing |
| title | Specific Y14 domains mediate its nucleo-cytoplasmic shuttling and association with spliced mRNA |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-07T11%3A19%3A36IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Specific%20Y14%20domains%20mediate%20its%20nucleo-cytoplasmic%20shuttling%20and%20association%20with%20spliced%20mRNA&rft.jtitle=Scientific%20reports&rft.au=Kataoka,%20Naoyuki&rft.date=2011-09-14&rft.volume=1&rft.issue=1&rft.spage=92&rft.epage=92&rft.pages=92-92&rft.artnum=92&rft.issn=2045-2322&rft.eissn=2045-2322&rft_id=info:doi/10.1038/srep00092&rft_dat=%3Cproquest_pubme%3E1897393402%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1897393402&rft_id=info:pmid/22355610&rfr_iscdi=true |