Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation
Snail1 is a central regulator of epithelial cell adhesion and movement in epithelial‐to‐mesenchymal transitions (EMTs) during embryo development; a process reactivated during cancer metastasis. While induction of Snail1 transcription precedes EMT induction, post‐translational regulation of Snail1 is...
Gespeichert in:
| Veröffentlicht in: | The EMBO journal 2012-01, Vol.31 (1), p.29-43 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext bestellen |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 43 |
|---|---|
| container_issue | 1 |
| container_start_page | 29 |
| container_title | The EMBO journal |
| container_volume | 31 |
| creator | Zhang, Kun Rodriguez-Aznar, Eva Yabuta, Norikazu Owen, Robert J Mingot, Jose M Nojima, Hiroshi Nieto, M Angela Longmore, Gregory D |
| description | Snail1 is a central regulator of epithelial cell adhesion and movement in epithelial‐to‐mesenchymal transitions (EMTs) during embryo development; a process reactivated during cancer metastasis. While induction of
Snail1
transcription precedes EMT induction, post‐translational regulation of Snail1 is also critical for determining Snail1's protein level, subcellular localization, and capacity to induce EMT. To identify novel post‐translational regulators of Snail1, we developed a live cell, bioluminescence‐based screen. From a human kinome RNAi screen, we have identified Lats2 kinase as a novel regulator of Snail1 protein level, subcellular localization, and thus, activity. We show that Lats2 interacts with Snail1 and directly phosphorylates Snail1 at residue T203. This occurs in the nucleus and serves to retain Snail1 in the nucleus thereby enhancing its stability. Lats2 was found to positively influence cellular EMT and tumour cell invasion, in a Snail1‐dependent manner. Indeed during TGFβ‐induced EMT Lats2 is activated and Snail1 phosphorylated at T203. Analysis in mouse and zebrafish embryo development confirms that Lats2 acts as a positive modulator of Snail1 protein level and potentiates its
in vivo
EMT activity.
The Lats2 kinase, a Hippo pathway component, is here shown to promote the epithelial–mesenchymal transition by phosphorylating the transcription factor Snail1. |
| doi_str_mv | 10.1038/emboj.2011.357 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_C6C</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3252572</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2633559811</sourcerecordid><originalsourceid>FETCH-LOGICAL-c5707-c971aac48f5f77e62bd8255884cc007e8c167d5995b763c847e45f65210b5cf83</originalsourceid><addsrcrecordid>eNptUc1v0zActRATKxtXjigSh53S2U78kQsSrbaVqTAkQEgIyXJcp3OX2MF2tuW_x11HNRAHf_7ee37-PQBeIzhFsOCnuqvdZoohQtOCsGdggkoKcwwZeQ4mEFOUl4hXh-BlCBsIIeEMvQCHGFUEw5JPwM-ljAFnN8bKoLPeRW2jkVGH7IuVpkWZVNHcmjhm9Zj13nUuGrvO7KBaLX3m9QPB2Wzo09Rfu5CGH1u5vTwGB41sg371uB6Bb-dnX-eLfHl18WH-fpkrwiDLVcWQlKrkDWkY0xTXK44J4bxUCkKmuUKUrUhVkZrRQvGS6ZI0lGAEa6IaXhyBdzvdfqg7vVLJkpet6L3ppB-Fk0b8XbHmWqzdrSgwwYThJHDyKODdr0GHKDoTlG5babUbgqhQiSvOOU3It_8gN27wNv1OoNRfzCiBVUK9eWpo7-RP3xOA7QB3ptXjvo6g2KYqHlIV21RFSlWcfZxdbg9pn5inO2ZIJLvW_qmB_7ETI98xTIj6fv-W9DeCsoIR8f3ThSCz-efF-eKHmBW_ARYNto4</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1000276509</pqid></control><display><type>article</type><title>Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation</title><source>Springer Nature OA Free Journals</source><creator>Zhang, Kun ; Rodriguez-Aznar, Eva ; Yabuta, Norikazu ; Owen, Robert J ; Mingot, Jose M ; Nojima, Hiroshi ; Nieto, M Angela ; Longmore, Gregory D</creator><creatorcontrib>Zhang, Kun ; Rodriguez-Aznar, Eva ; Yabuta, Norikazu ; Owen, Robert J ; Mingot, Jose M ; Nojima, Hiroshi ; Nieto, M Angela ; Longmore, Gregory D</creatorcontrib><description>Snail1 is a central regulator of epithelial cell adhesion and movement in epithelial‐to‐mesenchymal transitions (EMTs) during embryo development; a process reactivated during cancer metastasis. While induction of
Snail1
transcription precedes EMT induction, post‐translational regulation of Snail1 is also critical for determining Snail1's protein level, subcellular localization, and capacity to induce EMT. To identify novel post‐translational regulators of Snail1, we developed a live cell, bioluminescence‐based screen. From a human kinome RNAi screen, we have identified Lats2 kinase as a novel regulator of Snail1 protein level, subcellular localization, and thus, activity. We show that Lats2 interacts with Snail1 and directly phosphorylates Snail1 at residue T203. This occurs in the nucleus and serves to retain Snail1 in the nucleus thereby enhancing its stability. Lats2 was found to positively influence cellular EMT and tumour cell invasion, in a Snail1‐dependent manner. Indeed during TGFβ‐induced EMT Lats2 is activated and Snail1 phosphorylated at T203. Analysis in mouse and zebrafish embryo development confirms that Lats2 acts as a positive modulator of Snail1 protein level and potentiates its
in vivo
EMT activity.
The Lats2 kinase, a Hippo pathway component, is here shown to promote the epithelial–mesenchymal transition by phosphorylating the transcription factor Snail1.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/emboj.2011.357</identifier><identifier>PMID: 21952048</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Adhesion ; Amino Acid Sequence ; Animals ; Bioluminescence ; breast cancer ; Cell Nucleus - metabolism ; Cells, Cultured ; Dogs ; EMBO24 ; EMBO37 ; Embryo, Mammalian - metabolism ; Embryo, Nonmammalian - metabolism ; Embryos ; Epithelial-Mesenchymal Transition ; HCT116 Cells ; HEK293 Cells ; Humans ; Lats2 ; Mice ; Molecular Sequence Data ; Nuclear energy ; Phosphorylation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; RNA Interference ; Snail Family Transcription Factors ; Snail1 ; Transcription Factors - genetics ; Transcription Factors - metabolism ; Transfection ; Tumor Suppressor Proteins - genetics ; Tumor Suppressor Proteins - metabolism ; Zebrafish</subject><ispartof>The EMBO journal, 2012-01, Vol.31 (1), p.29-43</ispartof><rights>European Molecular Biology Organization 2012</rights><rights>Copyright © 2012 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Jan 4, 2012</rights><rights>Copyright © 2012, European Molecular Biology Organization 2012 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5707-c971aac48f5f77e62bd8255884cc007e8c167d5995b763c847e45f65210b5cf83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252572/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3252572/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,1427,27903,27904,41099,42168,45553,45554,46387,46811,51554,53769,53771</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/emboj.2011.357$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21952048$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Zhang, Kun</creatorcontrib><creatorcontrib>Rodriguez-Aznar, Eva</creatorcontrib><creatorcontrib>Yabuta, Norikazu</creatorcontrib><creatorcontrib>Owen, Robert J</creatorcontrib><creatorcontrib>Mingot, Jose M</creatorcontrib><creatorcontrib>Nojima, Hiroshi</creatorcontrib><creatorcontrib>Nieto, M Angela</creatorcontrib><creatorcontrib>Longmore, Gregory D</creatorcontrib><title>Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Snail1 is a central regulator of epithelial cell adhesion and movement in epithelial‐to‐mesenchymal transitions (EMTs) during embryo development; a process reactivated during cancer metastasis. While induction of
Snail1
transcription precedes EMT induction, post‐translational regulation of Snail1 is also critical for determining Snail1's protein level, subcellular localization, and capacity to induce EMT. To identify novel post‐translational regulators of Snail1, we developed a live cell, bioluminescence‐based screen. From a human kinome RNAi screen, we have identified Lats2 kinase as a novel regulator of Snail1 protein level, subcellular localization, and thus, activity. We show that Lats2 interacts with Snail1 and directly phosphorylates Snail1 at residue T203. This occurs in the nucleus and serves to retain Snail1 in the nucleus thereby enhancing its stability. Lats2 was found to positively influence cellular EMT and tumour cell invasion, in a Snail1‐dependent manner. Indeed during TGFβ‐induced EMT Lats2 is activated and Snail1 phosphorylated at T203. Analysis in mouse and zebrafish embryo development confirms that Lats2 acts as a positive modulator of Snail1 protein level and potentiates its
in vivo
EMT activity.
The Lats2 kinase, a Hippo pathway component, is here shown to promote the epithelial–mesenchymal transition by phosphorylating the transcription factor Snail1.</description><subject>Adhesion</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Bioluminescence</subject><subject>breast cancer</subject><subject>Cell Nucleus - metabolism</subject><subject>Cells, Cultured</subject><subject>Dogs</subject><subject>EMBO24</subject><subject>EMBO37</subject><subject>Embryo, Mammalian - metabolism</subject><subject>Embryo, Nonmammalian - metabolism</subject><subject>Embryos</subject><subject>Epithelial-Mesenchymal Transition</subject><subject>HCT116 Cells</subject><subject>HEK293 Cells</subject><subject>Humans</subject><subject>Lats2</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Nuclear energy</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteins</subject><subject>RNA Interference</subject><subject>Snail Family Transcription Factors</subject><subject>Snail1</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><subject>Transfection</subject><subject>Tumor Suppressor Proteins - genetics</subject><subject>Tumor Suppressor Proteins - metabolism</subject><subject>Zebrafish</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNptUc1v0zActRATKxtXjigSh53S2U78kQsSrbaVqTAkQEgIyXJcp3OX2MF2tuW_x11HNRAHf_7ee37-PQBeIzhFsOCnuqvdZoohQtOCsGdggkoKcwwZeQ4mEFOUl4hXh-BlCBsIIeEMvQCHGFUEw5JPwM-ljAFnN8bKoLPeRW2jkVGH7IuVpkWZVNHcmjhm9Zj13nUuGrvO7KBaLX3m9QPB2Wzo09Rfu5CGH1u5vTwGB41sg371uB6Bb-dnX-eLfHl18WH-fpkrwiDLVcWQlKrkDWkY0xTXK44J4bxUCkKmuUKUrUhVkZrRQvGS6ZI0lGAEa6IaXhyBdzvdfqg7vVLJkpet6L3ppB-Fk0b8XbHmWqzdrSgwwYThJHDyKODdr0GHKDoTlG5babUbgqhQiSvOOU3It_8gN27wNv1OoNRfzCiBVUK9eWpo7-RP3xOA7QB3ptXjvo6g2KYqHlIV21RFSlWcfZxdbg9pn5inO2ZIJLvW_qmB_7ETI98xTIj6fv-W9DeCsoIR8f3ThSCz-efF-eKHmBW_ARYNto4</recordid><startdate>20120104</startdate><enddate>20120104</enddate><creator>Zhang, Kun</creator><creator>Rodriguez-Aznar, Eva</creator><creator>Yabuta, Norikazu</creator><creator>Owen, Robert J</creator><creator>Mingot, Jose M</creator><creator>Nojima, Hiroshi</creator><creator>Nieto, M Angela</creator><creator>Longmore, Gregory D</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</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>BKSAR</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>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20120104</creationdate><title>Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation</title><author>Zhang, Kun ; Rodriguez-Aznar, Eva ; Yabuta, Norikazu ; Owen, Robert J ; Mingot, Jose M ; Nojima, Hiroshi ; Nieto, M Angela ; Longmore, Gregory D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5707-c971aac48f5f77e62bd8255884cc007e8c167d5995b763c847e45f65210b5cf83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Adhesion</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Bioluminescence</topic><topic>breast cancer</topic><topic>Cell Nucleus - metabolism</topic><topic>Cells, Cultured</topic><topic>Dogs</topic><topic>EMBO24</topic><topic>EMBO37</topic><topic>Embryo, Mammalian - metabolism</topic><topic>Embryo, Nonmammalian - metabolism</topic><topic>Embryos</topic><topic>Epithelial-Mesenchymal Transition</topic><topic>HCT116 Cells</topic><topic>HEK293 Cells</topic><topic>Humans</topic><topic>Lats2</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Nuclear energy</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>RNA Interference</topic><topic>Snail Family Transcription Factors</topic><topic>Snail1</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><topic>Transfection</topic><topic>Tumor Suppressor Proteins - genetics</topic><topic>Tumor Suppressor Proteins - metabolism</topic><topic>Zebrafish</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Zhang, Kun</creatorcontrib><creatorcontrib>Rodriguez-Aznar, Eva</creatorcontrib><creatorcontrib>Yabuta, Norikazu</creatorcontrib><creatorcontrib>Owen, Robert J</creatorcontrib><creatorcontrib>Mingot, Jose M</creatorcontrib><creatorcontrib>Nojima, Hiroshi</creatorcontrib><creatorcontrib>Nieto, M Angela</creatorcontrib><creatorcontrib>Longmore, Gregory D</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</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>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</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>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</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>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science 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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Zhang, Kun</au><au>Rodriguez-Aznar, Eva</au><au>Yabuta, Norikazu</au><au>Owen, Robert J</au><au>Mingot, Jose M</au><au>Nojima, Hiroshi</au><au>Nieto, M Angela</au><au>Longmore, Gregory D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2012-01-04</date><risdate>2012</risdate><volume>31</volume><issue>1</issue><spage>29</spage><epage>43</epage><pages>29-43</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>Snail1 is a central regulator of epithelial cell adhesion and movement in epithelial‐to‐mesenchymal transitions (EMTs) during embryo development; a process reactivated during cancer metastasis. While induction of
Snail1
transcription precedes EMT induction, post‐translational regulation of Snail1 is also critical for determining Snail1's protein level, subcellular localization, and capacity to induce EMT. To identify novel post‐translational regulators of Snail1, we developed a live cell, bioluminescence‐based screen. From a human kinome RNAi screen, we have identified Lats2 kinase as a novel regulator of Snail1 protein level, subcellular localization, and thus, activity. We show that Lats2 interacts with Snail1 and directly phosphorylates Snail1 at residue T203. This occurs in the nucleus and serves to retain Snail1 in the nucleus thereby enhancing its stability. Lats2 was found to positively influence cellular EMT and tumour cell invasion, in a Snail1‐dependent manner. Indeed during TGFβ‐induced EMT Lats2 is activated and Snail1 phosphorylated at T203. Analysis in mouse and zebrafish embryo development confirms that Lats2 acts as a positive modulator of Snail1 protein level and potentiates its
in vivo
EMT activity.
The Lats2 kinase, a Hippo pathway component, is here shown to promote the epithelial–mesenchymal transition by phosphorylating the transcription factor Snail1.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>21952048</pmid><doi>10.1038/emboj.2011.357</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext_linktorsrc |
| identifier | ISSN: 0261-4189 |
| ispartof | The EMBO journal, 2012-01, Vol.31 (1), p.29-43 |
| issn | 0261-4189 1460-2075 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3252572 |
| source | Springer Nature OA Free Journals |
| subjects | Adhesion Amino Acid Sequence Animals Bioluminescence breast cancer Cell Nucleus - metabolism Cells, Cultured Dogs EMBO24 EMBO37 Embryo, Mammalian - metabolism Embryo, Nonmammalian - metabolism Embryos Epithelial-Mesenchymal Transition HCT116 Cells HEK293 Cells Humans Lats2 Mice Molecular Sequence Data Nuclear energy Phosphorylation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Proteins RNA Interference Snail Family Transcription Factors Snail1 Transcription Factors - genetics Transcription Factors - metabolism Transfection Tumor Suppressor Proteins - genetics Tumor Suppressor Proteins - metabolism Zebrafish |
| title | Lats2 kinase potentiates Snail1 activity by promoting nuclear retention upon phosphorylation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T10%3A33%3A01IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_C6C&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Lats2%20kinase%20potentiates%20Snail1%20activity%20by%20promoting%20nuclear%20retention%20upon%20phosphorylation&rft.jtitle=The%20EMBO%20journal&rft.au=Zhang,%20Kun&rft.date=2012-01-04&rft.volume=31&rft.issue=1&rft.spage=29&rft.epage=43&rft.pages=29-43&rft.issn=0261-4189&rft.eissn=1460-2075&rft.coden=EMJODG&rft_id=info:doi/10.1038/emboj.2011.357&rft_dat=%3Cproquest_C6C%3E2633559811%3C/proquest_C6C%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1000276509&rft_id=info:pmid/21952048&rfr_iscdi=true |