Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis
let-7a, a miRNA involved in differentiation, was known to be regulated by Lin-28. Now work reveals another factor that could control let-7a levels in vivo : hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via...
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| Veröffentlicht in: | Nature structural & molecular biology 2010-08, Vol.17 (8), p.1011-1018 |
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| creator | Michlewski, Gracjan Cáceres, Javier F |
| description | let-7a, a miRNA involved in differentiation, was known to be regulated by Lin-28. Now work reveals another factor that could control let-7a levels
in vivo
: hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via antagonizing the binding of KSRP to pri-let-7a, which is known to promote biogenesis.
The pluripotency-promoting proteins Lin28a and Lin28b act as post-transcriptional repressors of let-7 miRNA biogenesis in undifferentiated embryonic stem cells. The levels of mature let-7a differ substantially in cells lacking Lin28 expression, indicating the existence of additional mechanism(s) of post-transcriptional regulation. Here, we present evidence supporting a role for heteronuclear ribonucleoprotein A1 (hnRNP A1) as a negative regulator of let-7a. HnRNP A1 binds the conserved terminal loop of pri-let-7a-1 and inhibits its processing by Drosha. Levels of mature let-7a negatively correlate with hnRNP A1 levels in somatic cell lines. Furthermore, hnRNP A1 depletion increased pri-let-7a-1 processing by cell extracts, whereas its ectopic expression decreased let-7a production
in vivo
. Finally, hnRNP A1 binding to let-7a interferes with the binding of KSRP, which is known to promote let-7a biogenesis. We propose that hnRNP A1 and KSRP have antagonistic roles in the post-transcriptional regulation of let-7a expression. |
| doi_str_mv | 10.1038/nsmb.1874 |
| format | Article |
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in vivo
: hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via antagonizing the binding of KSRP to pri-let-7a, which is known to promote biogenesis.
The pluripotency-promoting proteins Lin28a and Lin28b act as post-transcriptional repressors of let-7 miRNA biogenesis in undifferentiated embryonic stem cells. The levels of mature let-7a differ substantially in cells lacking Lin28 expression, indicating the existence of additional mechanism(s) of post-transcriptional regulation. Here, we present evidence supporting a role for heteronuclear ribonucleoprotein A1 (hnRNP A1) as a negative regulator of let-7a. HnRNP A1 binds the conserved terminal loop of pri-let-7a-1 and inhibits its processing by Drosha. Levels of mature let-7a negatively correlate with hnRNP A1 levels in somatic cell lines. Furthermore, hnRNP A1 depletion increased pri-let-7a-1 processing by cell extracts, whereas its ectopic expression decreased let-7a production
in vivo
. Finally, hnRNP A1 binding to let-7a interferes with the binding of KSRP, which is known to promote let-7a biogenesis. We propose that hnRNP A1 and KSRP have antagonistic roles in the post-transcriptional regulation of let-7a expression.</description><identifier>ISSN: 1545-9993</identifier><identifier>ISSN: 1545-9985</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.1874</identifier><identifier>PMID: 20639884</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/208/200 ; 631/337/1645 ; 631/337/384/331 ; 631/45/535 ; Base Sequence ; Binding sites ; Binding, Competitive ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Cell Line, Tumor ; DNA Footprinting ; Gene Expression Regulation, Neoplastic ; Genetic regulation ; Green Fluorescent Proteins - metabolism ; Heterogeneous Nuclear Ribonucleoprotein A1 ; Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics ; Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism ; Humans ; Life Sciences ; Membrane Biology ; MicroRNA ; MicroRNAs - biosynthesis ; MicroRNAs - chemistry ; MicroRNAs - genetics ; Models, Biological ; Molecular biology ; Molecular Sequence Data ; Molecular structure ; Nucleic Acid Conformation ; Physiological aspects ; Properties ; Protein Binding ; Protein Structure ; Proteins ; Recombinant Fusion Proteins - metabolism ; Ribonuclease III - metabolism ; RNA processing ; RNA Processing, Post-Transcriptional ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Stem cells ; Trans-Activators - genetics ; Trans-Activators - metabolism</subject><ispartof>Nature structural & molecular biology, 2010-08, Vol.17 (8), p.1011-1018</ispartof><rights>Springer Nature America, Inc. 2010</rights><rights>COPYRIGHT 2010 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Aug 2010</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-7910bae3b23843c7f39b1c4f783d71d0f950b1ae4f689c55251d27286af411e23</citedby><cites>FETCH-LOGICAL-c530t-7910bae3b23843c7f39b1c4f783d71d0f950b1ae4f689c55251d27286af411e23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb.1874$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb.1874$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>230,314,776,780,881,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20639884$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Michlewski, Gracjan</creatorcontrib><creatorcontrib>Cáceres, Javier F</creatorcontrib><title>Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>let-7a, a miRNA involved in differentiation, was known to be regulated by Lin-28. Now work reveals another factor that could control let-7a levels
in vivo
: hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via antagonizing the binding of KSRP to pri-let-7a, which is known to promote biogenesis.
The pluripotency-promoting proteins Lin28a and Lin28b act as post-transcriptional repressors of let-7 miRNA biogenesis in undifferentiated embryonic stem cells. The levels of mature let-7a differ substantially in cells lacking Lin28 expression, indicating the existence of additional mechanism(s) of post-transcriptional regulation. Here, we present evidence supporting a role for heteronuclear ribonucleoprotein A1 (hnRNP A1) as a negative regulator of let-7a. HnRNP A1 binds the conserved terminal loop of pri-let-7a-1 and inhibits its processing by Drosha. Levels of mature let-7a negatively correlate with hnRNP A1 levels in somatic cell lines. Furthermore, hnRNP A1 depletion increased pri-let-7a-1 processing by cell extracts, whereas its ectopic expression decreased let-7a production
in vivo
. Finally, hnRNP A1 binding to let-7a interferes with the binding of KSRP, which is known to promote let-7a biogenesis. We propose that hnRNP A1 and KSRP have antagonistic roles in the post-transcriptional regulation of let-7a expression.</description><subject>631/208/200</subject><subject>631/337/1645</subject><subject>631/337/384/331</subject><subject>631/45/535</subject><subject>Base Sequence</subject><subject>Binding sites</subject><subject>Binding, Competitive</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Line, Tumor</subject><subject>DNA Footprinting</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>Genetic regulation</subject><subject>Green Fluorescent Proteins - metabolism</subject><subject>Heterogeneous Nuclear Ribonucleoprotein A1</subject><subject>Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics</subject><subject>Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>MicroRNA</subject><subject>MicroRNAs - biosynthesis</subject><subject>MicroRNAs - chemistry</subject><subject>MicroRNAs - genetics</subject><subject>Models, Biological</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Molecular structure</subject><subject>Nucleic Acid Conformation</subject><subject>Physiological aspects</subject><subject>Properties</subject><subject>Protein Binding</subject><subject>Protein Structure</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Ribonuclease III - metabolism</subject><subject>RNA processing</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Stem cells</subject><subject>Trans-Activators - genetics</subject><subject>Trans-Activators - metabolism</subject><issn>1545-9993</issn><issn>1545-9985</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNplkV1rFTEQhoNYbK1e-Ack6IUonJrPTXIjHIofxaql6nXIZid7UvYkNdkV_Pfd5dSj1asE5plnZngRekLJCSVcv051255QrcQ9dESlkCtjtLy__xt-iB7WekUIk1LxB-iQkYYbrcUR-rROo-tzinWMHpc8AM4Bb9Ll5wu8ptilDn_8enmBY8LjBnCBfhrcGHNasAHGlXK4jbmHBDXWR-gguKHC49v3GH1_9_bb6YfV-Zf3Z6fr85WXnMw9hpLWAW8Z14J7FbhpqRdBad4p2pFgJGmpAxEabbyUTNKOKaYbFwSlwPgxerPzXk_tFjoPaSxusNclbl35ZbOL9m4lxY3t80_LDOOEiVnw4lZQ8o8J6mi3sXoYBpcgT9UqoY0QhC-jnv1DXuWppPk6q7hkQmu-6J7voN4NYGMKeZ7qF6VdMy4U5U2zUC93lC-51gJhvzAldgnSLkHaJciZffr3hXvyd3Iz8GoH1LmUeih_9vrfdgPcEKTl</recordid><startdate>20100801</startdate><enddate>20100801</enddate><creator>Michlewski, Gracjan</creator><creator>Cáceres, Javier F</creator><general>Nature Publishing Group US</general><general>Nature Publishing Group</general><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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20100801</creationdate><title>Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis</title><author>Michlewski, Gracjan ; Cáceres, Javier F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-7910bae3b23843c7f39b1c4f783d71d0f950b1ae4f689c55251d27286af411e23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>631/208/200</topic><topic>631/337/1645</topic><topic>631/337/384/331</topic><topic>631/45/535</topic><topic>Base Sequence</topic><topic>Binding sites</topic><topic>Binding, Competitive</topic><topic>Biochemistry</topic><topic>Biological Microscopy</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Line, Tumor</topic><topic>DNA Footprinting</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>Genetic regulation</topic><topic>Green Fluorescent Proteins - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Michlewski, Gracjan</au><au>Cáceres, Javier F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2010-08-01</date><risdate>2010</risdate><volume>17</volume><issue>8</issue><spage>1011</spage><epage>1018</epage><pages>1011-1018</pages><issn>1545-9993</issn><issn>1545-9985</issn><eissn>1545-9985</eissn><abstract>let-7a, a miRNA involved in differentiation, was known to be regulated by Lin-28. Now work reveals another factor that could control let-7a levels
in vivo
: hnRNP A1 binds to unprocessed pri-let-7a and inhibits its processing by Drosha. The inhibitory effect of hnRNP A1 is further shown to occur via antagonizing the binding of KSRP to pri-let-7a, which is known to promote biogenesis.
The pluripotency-promoting proteins Lin28a and Lin28b act as post-transcriptional repressors of let-7 miRNA biogenesis in undifferentiated embryonic stem cells. The levels of mature let-7a differ substantially in cells lacking Lin28 expression, indicating the existence of additional mechanism(s) of post-transcriptional regulation. Here, we present evidence supporting a role for heteronuclear ribonucleoprotein A1 (hnRNP A1) as a negative regulator of let-7a. HnRNP A1 binds the conserved terminal loop of pri-let-7a-1 and inhibits its processing by Drosha. Levels of mature let-7a negatively correlate with hnRNP A1 levels in somatic cell lines. Furthermore, hnRNP A1 depletion increased pri-let-7a-1 processing by cell extracts, whereas its ectopic expression decreased let-7a production
in vivo
. Finally, hnRNP A1 binding to let-7a interferes with the binding of KSRP, which is known to promote let-7a biogenesis. We propose that hnRNP A1 and KSRP have antagonistic roles in the post-transcriptional regulation of let-7a expression.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>20639884</pmid><doi>10.1038/nsmb.1874</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/208/200 631/337/1645 631/337/384/331 631/45/535 Base Sequence Binding sites Binding, Competitive Biochemistry Biological Microscopy Biomedical and Life Sciences Cell Line, Tumor DNA Footprinting Gene Expression Regulation, Neoplastic Genetic regulation Green Fluorescent Proteins - metabolism Heterogeneous Nuclear Ribonucleoprotein A1 Heterogeneous-Nuclear Ribonucleoprotein Group A-B - genetics Heterogeneous-Nuclear Ribonucleoprotein Group A-B - metabolism Humans Life Sciences Membrane Biology MicroRNA MicroRNAs - biosynthesis MicroRNAs - chemistry MicroRNAs - genetics Models, Biological Molecular biology Molecular Sequence Data Molecular structure Nucleic Acid Conformation Physiological aspects Properties Protein Binding Protein Structure Proteins Recombinant Fusion Proteins - metabolism Ribonuclease III - metabolism RNA processing RNA Processing, Post-Transcriptional RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Stem cells Trans-Activators - genetics Trans-Activators - metabolism |
| title | Antagonistic role of hnRNP A1 and KSRP in the regulation of let-7a biogenesis |
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