Translational Control of Putative Protooncogene Nm23-M2 by Cytokines via Phosphoinositide 3-Kinase Signaling
The expansion and differentiation of hematopoietic progenitors is regulated by cytokine and growth factor signaling. To examine how signal transduction controls the gene expression program required for progenitor expansion, we screened ATLAS filters with polysome-associated mRNA derived from erythro...
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| Veröffentlicht in: | The Journal of biological chemistry 2004-09, Vol.279 (37), p.38169-38176 |
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| creator | Joosten, Marieke Blázquez-Domingo, Montserrat Lindeboom, Fokke Boulmé, Florence Van Hoven-Beijen, Antoinette Habermann, Bianca Löwenberg, Bob Beug, Hartmut Müllner, Ernst W. Delwel, Ruud Von Lindern, Marieke |
| description | The expansion and differentiation of hematopoietic progenitors is regulated by cytokine and growth factor signaling. To examine how signal transduction controls the gene expression program required for progenitor expansion, we screened ATLAS filters with polysome-associated mRNA derived from erythroid progenitors stimulated with erythropoietin and/or stem cell factor. The putative proto-oncogene nucleoside diphosphate kinase B (ndpk-B or nm23-M2) was identified as an erythropoietin and stem cell factor target gene. Factor-induced expression of nm23-M2 was regulated specifically at the level of polysome association by a phosphoinositide 3-kinase-dependent mechanism. Identification of the transcription initiation site revealed that nm23-M2 mRNA starts with a terminal oligopyrimidine sequence, which is known to render mRNA translation dependent on mitogenic factors. Recently, the nm23-M2 locus was identified as a common leukemia retrovirus integration site, suggesting that it plays a role in leukemia development. The expression of Nm23 from a retroviral vector in the absence of its 5′-untranslated region caused constitutive polysome association of nm23-M2. Polysome-association and protein expression of endogenous nm23-M2 declined during differentiation of erythroid progenitors, suggesting a role for Nm23-M2 in progenitor expansion. Taken together, nm23-m2 exemplifies that cytokine-dependent control of translation initiation is an important mechanism of gene expression regulation. |
| doi_str_mv | 10.1074/jbc.M401283200 |
| format | Article |
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To examine how signal transduction controls the gene expression program required for progenitor expansion, we screened ATLAS filters with polysome-associated mRNA derived from erythroid progenitors stimulated with erythropoietin and/or stem cell factor. The putative proto-oncogene nucleoside diphosphate kinase B (ndpk-B or nm23-M2) was identified as an erythropoietin and stem cell factor target gene. Factor-induced expression of nm23-M2 was regulated specifically at the level of polysome association by a phosphoinositide 3-kinase-dependent mechanism. Identification of the transcription initiation site revealed that nm23-M2 mRNA starts with a terminal oligopyrimidine sequence, which is known to render mRNA translation dependent on mitogenic factors. Recently, the nm23-M2 locus was identified as a common leukemia retrovirus integration site, suggesting that it plays a role in leukemia development. The expression of Nm23 from a retroviral vector in the absence of its 5′-untranslated region caused constitutive polysome association of nm23-M2. Polysome-association and protein expression of endogenous nm23-M2 declined during differentiation of erythroid progenitors, suggesting a role for Nm23-M2 in progenitor expansion. Taken together, nm23-m2 exemplifies that cytokine-dependent control of translation initiation is an important mechanism of gene expression regulation.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M401283200</identifier><identifier>PMID: 15247270</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>5' Untranslated Regions ; Animals ; Base Sequence ; Blotting, Northern ; Cell Differentiation ; Cells, Cultured ; Cloning, Molecular ; DNA Primers - chemistry ; DNA, Complementary - metabolism ; Down-Regulation ; Erythropoietin - metabolism ; Gene Deletion ; Gene Expression Regulation ; Gene Expression Regulation, Enzymologic ; Genetic Vectors ; Mice ; Molecular Sequence Data ; NM23 Nucleoside Diphosphate Kinases ; Nucleic Acid Conformation ; Nucleoside-Diphosphate Kinase - genetics ; Nucleoside-Diphosphate Kinase - metabolism ; Oligonucleotide Array Sequence Analysis ; Phosphatidylinositol 3-Kinases - metabolism ; Poly A - metabolism ; Polyribosomes - metabolism ; Protein Biosynthesis ; Pyrimidines - chemistry ; Retroviridae - genetics ; Reverse Transcriptase Polymerase Chain Reaction ; RNA, Messenger - metabolism ; Signal Transduction ; Stem Cell Factor - metabolism ; Time Factors ; Up-Regulation</subject><ispartof>The Journal of biological chemistry, 2004-09, Vol.279 (37), p.38169-38176</ispartof><rights>2004 © 2004 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-b2ccb11aa6539581e5e87875d18a619f47a874a0a886fd15e7407ab3de7ea3393</citedby><cites>FETCH-LOGICAL-c440t-b2ccb11aa6539581e5e87875d18a619f47a874a0a886fd15e7407ab3de7ea3393</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15247270$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Joosten, Marieke</creatorcontrib><creatorcontrib>Blázquez-Domingo, Montserrat</creatorcontrib><creatorcontrib>Lindeboom, Fokke</creatorcontrib><creatorcontrib>Boulmé, Florence</creatorcontrib><creatorcontrib>Van Hoven-Beijen, Antoinette</creatorcontrib><creatorcontrib>Habermann, Bianca</creatorcontrib><creatorcontrib>Löwenberg, Bob</creatorcontrib><creatorcontrib>Beug, Hartmut</creatorcontrib><creatorcontrib>Müllner, Ernst W.</creatorcontrib><creatorcontrib>Delwel, Ruud</creatorcontrib><creatorcontrib>Von Lindern, Marieke</creatorcontrib><title>Translational Control of Putative Protooncogene Nm23-M2 by Cytokines via Phosphoinositide 3-Kinase Signaling</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The expansion and differentiation of hematopoietic progenitors is regulated by cytokine and growth factor signaling. To examine how signal transduction controls the gene expression program required for progenitor expansion, we screened ATLAS filters with polysome-associated mRNA derived from erythroid progenitors stimulated with erythropoietin and/or stem cell factor. The putative proto-oncogene nucleoside diphosphate kinase B (ndpk-B or nm23-M2) was identified as an erythropoietin and stem cell factor target gene. Factor-induced expression of nm23-M2 was regulated specifically at the level of polysome association by a phosphoinositide 3-kinase-dependent mechanism. Identification of the transcription initiation site revealed that nm23-M2 mRNA starts with a terminal oligopyrimidine sequence, which is known to render mRNA translation dependent on mitogenic factors. Recently, the nm23-M2 locus was identified as a common leukemia retrovirus integration site, suggesting that it plays a role in leukemia development. The expression of Nm23 from a retroviral vector in the absence of its 5′-untranslated region caused constitutive polysome association of nm23-M2. Polysome-association and protein expression of endogenous nm23-M2 declined during differentiation of erythroid progenitors, suggesting a role for Nm23-M2 in progenitor expansion. Taken together, nm23-m2 exemplifies that cytokine-dependent control of translation initiation is an important mechanism of gene expression regulation.</description><subject>5' Untranslated Regions</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cell Differentiation</subject><subject>Cells, Cultured</subject><subject>Cloning, Molecular</subject><subject>DNA Primers - chemistry</subject><subject>DNA, Complementary - metabolism</subject><subject>Down-Regulation</subject><subject>Erythropoietin - metabolism</subject><subject>Gene Deletion</subject><subject>Gene Expression Regulation</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Genetic Vectors</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>NM23 Nucleoside Diphosphate Kinases</subject><subject>Nucleic Acid Conformation</subject><subject>Nucleoside-Diphosphate Kinase - genetics</subject><subject>Nucleoside-Diphosphate Kinase - metabolism</subject><subject>Oligonucleotide Array Sequence Analysis</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Poly A - metabolism</subject><subject>Polyribosomes - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Pyrimidines - chemistry</subject><subject>Retroviridae - genetics</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>RNA, Messenger - metabolism</subject><subject>Signal Transduction</subject><subject>Stem Cell Factor - metabolism</subject><subject>Time Factors</subject><subject>Up-Regulation</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1rGzEQhkVpaNw01x6LDqW3dfS1K-2xmLYpTVpDU8hNaLWzXqW7kiPJDv73VbAhp85lYHjel-FB6D0lS0qkuHro7PJWEMoUZ4S8QgtKFK94Te9fowUhjFYtq9U5epvSAykjWvoGndOaCckkWaDpLhqfJpNd8GbCq-BzDBMOA17vcrnuAa9jyCF4GzbgAf-cGa9uGe4OeHXI4a_zkPDeGbweQ9qOwfmQXHY9YF79cN4kwL_dpnQ7v3mHzgYzJbg87Qv05-uXu9V1dfPr2_fV55vKCkFy1TFrO0qNaWre1opCDUoqWfdUmYa2g5BGSWGIUaoZelqDFESajvcgwXDe8gv06di7jeFxBynr2SUL02Q8hF3SVCpFJW8KuDyCNoaUIgx6G91s4kFTop_96uJXv_gtgQ-n5l03Q_-Cn4QW4OMRGN1mfHIRdOeCHWHWTLaaS80VbZ4_VEcMioa9g6iTdeAt9CVis-6D-98L_wB1X5VF</recordid><startdate>20040910</startdate><enddate>20040910</enddate><creator>Joosten, Marieke</creator><creator>Blázquez-Domingo, Montserrat</creator><creator>Lindeboom, Fokke</creator><creator>Boulmé, Florence</creator><creator>Van Hoven-Beijen, Antoinette</creator><creator>Habermann, Bianca</creator><creator>Löwenberg, Bob</creator><creator>Beug, Hartmut</creator><creator>Müllner, Ernst W.</creator><creator>Delwel, Ruud</creator><creator>Von Lindern, Marieke</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>H94</scope></search><sort><creationdate>20040910</creationdate><title>Translational Control of Putative Protooncogene Nm23-M2 by Cytokines via Phosphoinositide 3-Kinase Signaling</title><author>Joosten, Marieke ; Blázquez-Domingo, Montserrat ; Lindeboom, Fokke ; Boulmé, Florence ; Van Hoven-Beijen, Antoinette ; Habermann, Bianca ; Löwenberg, Bob ; Beug, Hartmut ; Müllner, Ernst W. ; Delwel, Ruud ; Von Lindern, Marieke</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-b2ccb11aa6539581e5e87875d18a619f47a874a0a886fd15e7407ab3de7ea3393</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>5' Untranslated Regions</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cell Differentiation</topic><topic>Cells, Cultured</topic><topic>Cloning, Molecular</topic><topic>DNA Primers - chemistry</topic><topic>DNA, Complementary - metabolism</topic><topic>Down-Regulation</topic><topic>Erythropoietin - metabolism</topic><topic>Gene Deletion</topic><topic>Gene Expression Regulation</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Genetic Vectors</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>NM23 Nucleoside Diphosphate Kinases</topic><topic>Nucleic Acid Conformation</topic><topic>Nucleoside-Diphosphate Kinase - genetics</topic><topic>Nucleoside-Diphosphate Kinase - metabolism</topic><topic>Oligonucleotide Array Sequence Analysis</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Poly A - metabolism</topic><topic>Polyribosomes - metabolism</topic><topic>Protein Biosynthesis</topic><topic>Pyrimidines - chemistry</topic><topic>Retroviridae - genetics</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>RNA, Messenger - metabolism</topic><topic>Signal Transduction</topic><topic>Stem Cell Factor - metabolism</topic><topic>Time Factors</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joosten, Marieke</creatorcontrib><creatorcontrib>Blázquez-Domingo, Montserrat</creatorcontrib><creatorcontrib>Lindeboom, Fokke</creatorcontrib><creatorcontrib>Boulmé, Florence</creatorcontrib><creatorcontrib>Van Hoven-Beijen, Antoinette</creatorcontrib><creatorcontrib>Habermann, Bianca</creatorcontrib><creatorcontrib>Löwenberg, Bob</creatorcontrib><creatorcontrib>Beug, Hartmut</creatorcontrib><creatorcontrib>Müllner, Ernst W.</creatorcontrib><creatorcontrib>Delwel, Ruud</creatorcontrib><creatorcontrib>Von Lindern, Marieke</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joosten, Marieke</au><au>Blázquez-Domingo, Montserrat</au><au>Lindeboom, Fokke</au><au>Boulmé, Florence</au><au>Van Hoven-Beijen, Antoinette</au><au>Habermann, Bianca</au><au>Löwenberg, Bob</au><au>Beug, Hartmut</au><au>Müllner, Ernst W.</au><au>Delwel, Ruud</au><au>Von Lindern, Marieke</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Translational Control of Putative Protooncogene Nm23-M2 by Cytokines via Phosphoinositide 3-Kinase Signaling</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2004-09-10</date><risdate>2004</risdate><volume>279</volume><issue>37</issue><spage>38169</spage><epage>38176</epage><pages>38169-38176</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The expansion and differentiation of hematopoietic progenitors is regulated by cytokine and growth factor signaling. To examine how signal transduction controls the gene expression program required for progenitor expansion, we screened ATLAS filters with polysome-associated mRNA derived from erythroid progenitors stimulated with erythropoietin and/or stem cell factor. The putative proto-oncogene nucleoside diphosphate kinase B (ndpk-B or nm23-M2) was identified as an erythropoietin and stem cell factor target gene. Factor-induced expression of nm23-M2 was regulated specifically at the level of polysome association by a phosphoinositide 3-kinase-dependent mechanism. Identification of the transcription initiation site revealed that nm23-M2 mRNA starts with a terminal oligopyrimidine sequence, which is known to render mRNA translation dependent on mitogenic factors. Recently, the nm23-M2 locus was identified as a common leukemia retrovirus integration site, suggesting that it plays a role in leukemia development. The expression of Nm23 from a retroviral vector in the absence of its 5′-untranslated region caused constitutive polysome association of nm23-M2. Polysome-association and protein expression of endogenous nm23-M2 declined during differentiation of erythroid progenitors, suggesting a role for Nm23-M2 in progenitor expansion. Taken together, nm23-m2 exemplifies that cytokine-dependent control of translation initiation is an important mechanism of gene expression regulation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>15247270</pmid><doi>10.1074/jbc.M401283200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2004-09, Vol.279 (37), p.38169-38176 |
| issn | 0021-9258 1083-351X |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | 5' Untranslated Regions Animals Base Sequence Blotting, Northern Cell Differentiation Cells, Cultured Cloning, Molecular DNA Primers - chemistry DNA, Complementary - metabolism Down-Regulation Erythropoietin - metabolism Gene Deletion Gene Expression Regulation Gene Expression Regulation, Enzymologic Genetic Vectors Mice Molecular Sequence Data NM23 Nucleoside Diphosphate Kinases Nucleic Acid Conformation Nucleoside-Diphosphate Kinase - genetics Nucleoside-Diphosphate Kinase - metabolism Oligonucleotide Array Sequence Analysis Phosphatidylinositol 3-Kinases - metabolism Poly A - metabolism Polyribosomes - metabolism Protein Biosynthesis Pyrimidines - chemistry Retroviridae - genetics Reverse Transcriptase Polymerase Chain Reaction RNA, Messenger - metabolism Signal Transduction Stem Cell Factor - metabolism Time Factors Up-Regulation |
| title | Translational Control of Putative Protooncogene Nm23-M2 by Cytokines via Phosphoinositide 3-Kinase Signaling |
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