Loading…

Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells

STAT transcription factors are induced by a number of growth factors and cytokines. Within minutes of induction, the STAT proteins are phosphorylated on tyrosine and serine residues and translocated to the nucleus, where they bind to their DNA targets. The leukemia inhibitory factor (LIF) mediates p...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of cell biology 1997-09, Vol.138 (6), p.1207-1217
Main Authors: Boeuf, Hélène, Hauss, Charlotte, De Graeve, Fabienne, Baran, Nathalie, Kedinger, Claude
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93
cites cdi_FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93
container_end_page 1217
container_issue 6
container_start_page 1207
container_title The Journal of cell biology
container_volume 138
creator Boeuf, Hélène
Hauss, Charlotte
De Graeve, Fabienne
Baran, Nathalie
Kedinger, Claude
description STAT transcription factors are induced by a number of growth factors and cytokines. Within minutes of induction, the STAT proteins are phosphorylated on tyrosine and serine residues and translocated to the nucleus, where they bind to their DNA targets. The leukemia inhibitory factor (LIF) mediates pleiotropic and sometimes opposite effects both in vivo and in cultured cells. It is known, for example, to prevent differentiation of embryonic stem (ES) cells in vitro. To get insights into LIF-regulated signaling in ES cells, we have analyzed protein-binding and transcriptional properties of STAT recognition sites in ES cells cultivated in the presence and in the absence of LIF. We have detected a specific LIF-regulated DNA-binding activity implicating the STAT3 protein. We show that STAT3 phosphorylation is essential for this LIF-dependent DNA-binding activity. The possibility that ERK2 or a closely related protein kinase, whose activity is modulated in a LIF-dependent manner, contributes to this phosphorylation is discussed. Finally, we show that the multimerized STAT3-binding DNA element confers LIF responsiveness to a minimal thymidine kinase promoter. This, together with our observation that overexpression of STAT3 dominant-negative mutants abrogates this LIF responsiveness, clearly indicates that STAT3 is involved in LIF-regulated transcriptional events in ES cells. Finally, stable expression of such a dominant negative mutant of STAT3 induces morphological differentiation of ES cells despite continuous LIF supply. Our results suggest that STAT3 is a critical target of the LIF signaling pathway, which maintains pluripotent cell proliferation.
doi_str_mv 10.1083/jcb.138.6.1207
format article
fullrecord <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2132559</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1618164</jstor_id><sourcerecordid>1618164</sourcerecordid><originalsourceid>FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93</originalsourceid><addsrcrecordid>eNpdkUtr3DAUhUVpSSZpt101YLLIzq7etjeFMM0LBrpoSpfiStY0mtrSRLID8-8rM0PSZHWRztHh6H4IfSa4IrhhXzdGV4Q1lawIxfU7tCCC47IhHL9HC4wpKVtBxTE6SWmDMeY1Z0foqKVt09b1Av1e2emvHRwUd_7BaTeGuCuuweRZfrdb6zvrx-I-gk8muu3ogoe-uDSje4L5UDhfXA067oJ3pvg52qFY2r5PH9GHNfTJfjrMU_Tr-up-eVuuftzcLS9XpREMj6XugADjtYS1EYTrGlttdNvJFjrQ-YpC2xm85hRraIjkwIQ0wmpOOeemZafo2z53O-nBdia3jdCrbXQDxJ0K4NRrxbsH9Sc8KUoYFWIOuDgExPA42TSqwSWTvwDehikpIhklRIpsPH9j3IQp5m2knFVjKRmT2VTtTSaGlKJdPzchWM28VOalMi8l1cwrPzj7v_-z_QAo61_2-iZlJC9pkszbYP8Adk-cog</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>217066336</pqid></control><display><type>article</type><title>Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells</title><source>Alma/SFX Local Collection</source><creator>Boeuf, Hélène ; Hauss, Charlotte ; De Graeve, Fabienne ; Baran, Nathalie ; Kedinger, Claude</creator><creatorcontrib>Boeuf, Hélène ; Hauss, Charlotte ; De Graeve, Fabienne ; Baran, Nathalie ; Kedinger, Claude</creatorcontrib><description>STAT transcription factors are induced by a number of growth factors and cytokines. Within minutes of induction, the STAT proteins are phosphorylated on tyrosine and serine residues and translocated to the nucleus, where they bind to their DNA targets. The leukemia inhibitory factor (LIF) mediates pleiotropic and sometimes opposite effects both in vivo and in cultured cells. It is known, for example, to prevent differentiation of embryonic stem (ES) cells in vitro. To get insights into LIF-regulated signaling in ES cells, we have analyzed protein-binding and transcriptional properties of STAT recognition sites in ES cells cultivated in the presence and in the absence of LIF. We have detected a specific LIF-regulated DNA-binding activity implicating the STAT3 protein. We show that STAT3 phosphorylation is essential for this LIF-dependent DNA-binding activity. The possibility that ERK2 or a closely related protein kinase, whose activity is modulated in a LIF-dependent manner, contributes to this phosphorylation is discussed. Finally, we show that the multimerized STAT3-binding DNA element confers LIF responsiveness to a minimal thymidine kinase promoter. This, together with our observation that overexpression of STAT3 dominant-negative mutants abrogates this LIF responsiveness, clearly indicates that STAT3 is involved in LIF-regulated transcriptional events in ES cells. Finally, stable expression of such a dominant negative mutant of STAT3 induces morphological differentiation of ES cells despite continuous LIF supply. Our results suggest that STAT3 is a critical target of the LIF signaling pathway, which maintains pluripotent cell proliferation.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.138.6.1207</identifier><identifier>PMID: 9298977</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Acute-Phase Proteins - metabolism ; Animals ; Antibodies ; Antibody Specificity ; Binding Sites - physiology ; Blastocyst - cytology ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Cell Differentiation - drug effects ; Cell Differentiation - genetics ; Cell Division - drug effects ; Cell Division - genetics ; Cell Line ; Cell lines ; Cells ; Cellular biology ; Cellular differentiation ; DNA-Binding Proteins - immunology ; DNA-Binding Proteins - metabolism ; Embryonic stem cells ; Embryos ; Gene Expression Regulation, Developmental - drug effects ; Gene Expression Regulation, Enzymologic - drug effects ; Growth Inhibitors - chemistry ; Growth Inhibitors - genetics ; Growth Inhibitors - pharmacology ; Interleukin-6 ; Leukemia ; Leukemia Inhibitory Factor ; Lymphokines - chemistry ; Lymphokines - genetics ; Lymphokines - pharmacology ; Mice ; Mitogen-Activated Protein Kinase 1 ; Mutagenesis - physiology ; Myeloid cells ; PC12 cells ; Phosphoproteins - immunology ; Phosphorylation ; Pluripotent stem cells ; Promoter Regions, Genetic - drug effects ; Promoter Regions, Genetic - physiology ; Protein-Serine-Threonine Kinases - metabolism ; Proteins ; Proto-Oncogene Proteins c-fos - genetics ; Recombinant Fusion Proteins - genetics ; STAT3 Transcription Factor ; Stem cells ; Stem Cells - chemistry ; Stem Cells - cytology ; Stem Cells - enzymology ; Trans-Activators - immunology ; Trans-Activators - metabolism ; Transcription, Genetic - drug effects ; Tyrosine - metabolism</subject><ispartof>The Journal of cell biology, 1997-09, Vol.138 (6), p.1207-1217</ispartof><rights>Copyright 1997 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press Sep 22, 1997</rights><rights>1997</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93</citedby><cites>FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9298977$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Boeuf, Hélène</creatorcontrib><creatorcontrib>Hauss, Charlotte</creatorcontrib><creatorcontrib>De Graeve, Fabienne</creatorcontrib><creatorcontrib>Baran, Nathalie</creatorcontrib><creatorcontrib>Kedinger, Claude</creatorcontrib><title>Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>STAT transcription factors are induced by a number of growth factors and cytokines. Within minutes of induction, the STAT proteins are phosphorylated on tyrosine and serine residues and translocated to the nucleus, where they bind to their DNA targets. The leukemia inhibitory factor (LIF) mediates pleiotropic and sometimes opposite effects both in vivo and in cultured cells. It is known, for example, to prevent differentiation of embryonic stem (ES) cells in vitro. To get insights into LIF-regulated signaling in ES cells, we have analyzed protein-binding and transcriptional properties of STAT recognition sites in ES cells cultivated in the presence and in the absence of LIF. We have detected a specific LIF-regulated DNA-binding activity implicating the STAT3 protein. We show that STAT3 phosphorylation is essential for this LIF-dependent DNA-binding activity. The possibility that ERK2 or a closely related protein kinase, whose activity is modulated in a LIF-dependent manner, contributes to this phosphorylation is discussed. Finally, we show that the multimerized STAT3-binding DNA element confers LIF responsiveness to a minimal thymidine kinase promoter. This, together with our observation that overexpression of STAT3 dominant-negative mutants abrogates this LIF responsiveness, clearly indicates that STAT3 is involved in LIF-regulated transcriptional events in ES cells. Finally, stable expression of such a dominant negative mutant of STAT3 induces morphological differentiation of ES cells despite continuous LIF supply. Our results suggest that STAT3 is a critical target of the LIF signaling pathway, which maintains pluripotent cell proliferation.</description><subject>Acute-Phase Proteins - metabolism</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Antibody Specificity</subject><subject>Binding Sites - physiology</subject><subject>Blastocyst - cytology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</subject><subject>Cell Differentiation - drug effects</subject><subject>Cell Differentiation - genetics</subject><subject>Cell Division - drug effects</subject><subject>Cell Division - genetics</subject><subject>Cell Line</subject><subject>Cell lines</subject><subject>Cells</subject><subject>Cellular biology</subject><subject>Cellular differentiation</subject><subject>DNA-Binding Proteins - immunology</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Embryonic stem cells</subject><subject>Embryos</subject><subject>Gene Expression Regulation, Developmental - drug effects</subject><subject>Gene Expression Regulation, Enzymologic - drug effects</subject><subject>Growth Inhibitors - chemistry</subject><subject>Growth Inhibitors - genetics</subject><subject>Growth Inhibitors - pharmacology</subject><subject>Interleukin-6</subject><subject>Leukemia</subject><subject>Leukemia Inhibitory Factor</subject><subject>Lymphokines - chemistry</subject><subject>Lymphokines - genetics</subject><subject>Lymphokines - pharmacology</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinase 1</subject><subject>Mutagenesis - physiology</subject><subject>Myeloid cells</subject><subject>PC12 cells</subject><subject>Phosphoproteins - immunology</subject><subject>Phosphorylation</subject><subject>Pluripotent stem cells</subject><subject>Promoter Regions, Genetic - drug effects</subject><subject>Promoter Regions, Genetic - physiology</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-fos - genetics</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>STAT3 Transcription Factor</subject><subject>Stem cells</subject><subject>Stem Cells - chemistry</subject><subject>Stem Cells - cytology</subject><subject>Stem Cells - enzymology</subject><subject>Trans-Activators - immunology</subject><subject>Trans-Activators - metabolism</subject><subject>Transcription, Genetic - drug effects</subject><subject>Tyrosine - metabolism</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNpdkUtr3DAUhUVpSSZpt101YLLIzq7etjeFMM0LBrpoSpfiStY0mtrSRLID8-8rM0PSZHWRztHh6H4IfSa4IrhhXzdGV4Q1lawIxfU7tCCC47IhHL9HC4wpKVtBxTE6SWmDMeY1Z0foqKVt09b1Av1e2emvHRwUd_7BaTeGuCuuweRZfrdb6zvrx-I-gk8muu3ogoe-uDSje4L5UDhfXA067oJ3pvg52qFY2r5PH9GHNfTJfjrMU_Tr-up-eVuuftzcLS9XpREMj6XugADjtYS1EYTrGlttdNvJFjrQ-YpC2xm85hRraIjkwIQ0wmpOOeemZafo2z53O-nBdia3jdCrbXQDxJ0K4NRrxbsH9Sc8KUoYFWIOuDgExPA42TSqwSWTvwDehikpIhklRIpsPH9j3IQp5m2knFVjKRmT2VTtTSaGlKJdPzchWM28VOalMi8l1cwrPzj7v_-z_QAo61_2-iZlJC9pkszbYP8Adk-cog</recordid><startdate>19970922</startdate><enddate>19970922</enddate><creator>Boeuf, Hélène</creator><creator>Hauss, Charlotte</creator><creator>De Graeve, Fabienne</creator><creator>Baran, Nathalie</creator><creator>Kedinger, Claude</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19970922</creationdate><title>Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells</title><author>Boeuf, Hélène ; Hauss, Charlotte ; De Graeve, Fabienne ; Baran, Nathalie ; Kedinger, Claude</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Acute-Phase Proteins - metabolism</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Antibody Specificity</topic><topic>Binding Sites - physiology</topic><topic>Blastocyst - cytology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - metabolism</topic><topic>Cell Differentiation - drug effects</topic><topic>Cell Differentiation - genetics</topic><topic>Cell Division - drug effects</topic><topic>Cell Division - genetics</topic><topic>Cell Line</topic><topic>Cell lines</topic><topic>Cells</topic><topic>Cellular biology</topic><topic>Cellular differentiation</topic><topic>DNA-Binding Proteins - immunology</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Embryonic stem cells</topic><topic>Embryos</topic><topic>Gene Expression Regulation, Developmental - drug effects</topic><topic>Gene Expression Regulation, Enzymologic - drug effects</topic><topic>Growth Inhibitors - chemistry</topic><topic>Growth Inhibitors - genetics</topic><topic>Growth Inhibitors - pharmacology</topic><topic>Interleukin-6</topic><topic>Leukemia</topic><topic>Leukemia Inhibitory Factor</topic><topic>Lymphokines - chemistry</topic><topic>Lymphokines - genetics</topic><topic>Lymphokines - pharmacology</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinase 1</topic><topic>Mutagenesis - physiology</topic><topic>Myeloid cells</topic><topic>PC12 cells</topic><topic>Phosphoproteins - immunology</topic><topic>Phosphorylation</topic><topic>Pluripotent stem cells</topic><topic>Promoter Regions, Genetic - drug effects</topic><topic>Promoter Regions, Genetic - physiology</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-fos - genetics</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>STAT3 Transcription Factor</topic><topic>Stem cells</topic><topic>Stem Cells - chemistry</topic><topic>Stem Cells - cytology</topic><topic>Stem Cells - enzymology</topic><topic>Trans-Activators - immunology</topic><topic>Trans-Activators - metabolism</topic><topic>Transcription, Genetic - drug effects</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Boeuf, Hélène</creatorcontrib><creatorcontrib>Hauss, Charlotte</creatorcontrib><creatorcontrib>De Graeve, Fabienne</creatorcontrib><creatorcontrib>Baran, Nathalie</creatorcontrib><creatorcontrib>Kedinger, Claude</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Boeuf, Hélène</au><au>Hauss, Charlotte</au><au>De Graeve, Fabienne</au><au>Baran, Nathalie</au><au>Kedinger, Claude</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1997-09-22</date><risdate>1997</risdate><volume>138</volume><issue>6</issue><spage>1207</spage><epage>1217</epage><pages>1207-1217</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>STAT transcription factors are induced by a number of growth factors and cytokines. Within minutes of induction, the STAT proteins are phosphorylated on tyrosine and serine residues and translocated to the nucleus, where they bind to their DNA targets. The leukemia inhibitory factor (LIF) mediates pleiotropic and sometimes opposite effects both in vivo and in cultured cells. It is known, for example, to prevent differentiation of embryonic stem (ES) cells in vitro. To get insights into LIF-regulated signaling in ES cells, we have analyzed protein-binding and transcriptional properties of STAT recognition sites in ES cells cultivated in the presence and in the absence of LIF. We have detected a specific LIF-regulated DNA-binding activity implicating the STAT3 protein. We show that STAT3 phosphorylation is essential for this LIF-dependent DNA-binding activity. The possibility that ERK2 or a closely related protein kinase, whose activity is modulated in a LIF-dependent manner, contributes to this phosphorylation is discussed. Finally, we show that the multimerized STAT3-binding DNA element confers LIF responsiveness to a minimal thymidine kinase promoter. This, together with our observation that overexpression of STAT3 dominant-negative mutants abrogates this LIF responsiveness, clearly indicates that STAT3 is involved in LIF-regulated transcriptional events in ES cells. Finally, stable expression of such a dominant negative mutant of STAT3 induces morphological differentiation of ES cells despite continuous LIF supply. Our results suggest that STAT3 is a critical target of the LIF signaling pathway, which maintains pluripotent cell proliferation.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>9298977</pmid><doi>10.1083/jcb.138.6.1207</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0021-9525
ispartof The Journal of cell biology, 1997-09, Vol.138 (6), p.1207-1217
issn 0021-9525
1540-8140
language eng
recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2132559
source Alma/SFX Local Collection
subjects Acute-Phase Proteins - metabolism
Animals
Antibodies
Antibody Specificity
Binding Sites - physiology
Blastocyst - cytology
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Cell Differentiation - drug effects
Cell Differentiation - genetics
Cell Division - drug effects
Cell Division - genetics
Cell Line
Cell lines
Cells
Cellular biology
Cellular differentiation
DNA-Binding Proteins - immunology
DNA-Binding Proteins - metabolism
Embryonic stem cells
Embryos
Gene Expression Regulation, Developmental - drug effects
Gene Expression Regulation, Enzymologic - drug effects
Growth Inhibitors - chemistry
Growth Inhibitors - genetics
Growth Inhibitors - pharmacology
Interleukin-6
Leukemia
Leukemia Inhibitory Factor
Lymphokines - chemistry
Lymphokines - genetics
Lymphokines - pharmacology
Mice
Mitogen-Activated Protein Kinase 1
Mutagenesis - physiology
Myeloid cells
PC12 cells
Phosphoproteins - immunology
Phosphorylation
Pluripotent stem cells
Promoter Regions, Genetic - drug effects
Promoter Regions, Genetic - physiology
Protein-Serine-Threonine Kinases - metabolism
Proteins
Proto-Oncogene Proteins c-fos - genetics
Recombinant Fusion Proteins - genetics
STAT3 Transcription Factor
Stem cells
Stem Cells - chemistry
Stem Cells - cytology
Stem Cells - enzymology
Trans-Activators - immunology
Trans-Activators - metabolism
Transcription, Genetic - drug effects
Tyrosine - metabolism
title Leukemia Inhibitory Factor-Dependent Transcriptional Activation in Embryonic Stem Cells
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T18%3A19%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Leukemia%20Inhibitory%20Factor-Dependent%20Transcriptional%20Activation%20in%20Embryonic%20Stem%20Cells&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Boeuf,%20H%C3%A9l%C3%A8ne&rft.date=1997-09-22&rft.volume=138&rft.issue=6&rft.spage=1207&rft.epage=1217&rft.pages=1207-1217&rft.issn=0021-9525&rft.eissn=1540-8140&rft.coden=JCLBA3&rft_id=info:doi/10.1083/jcb.138.6.1207&rft_dat=%3Cjstor_pubme%3E1618164%3C/jstor_pubme%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c530t-bda1a3476afc514b70ebcb9d69adabc512a9dc0f420ba8164a356c5eb42444c93%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=217066336&rft_id=info:pmid/9298977&rft_jstor_id=1618164&rfr_iscdi=true