Induction of a Nerve Growth Factor‐Sensitive Kinase that Phosphorylates the DNA‐Binding Domain of the Orphan Nuclear Receptor NGFI‐B
: Nerve growth factor (NGF) induces the synthesis and the phosphorylation of the orphan nuclear receptor NGFI‐B in PC12 cells. Previous work has shown that phosphorylation, by protein kinase A, of a specific serine in the DNA‐binding domain inhibits its binding to the NGFI‐B response element. Also,...
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| Veröffentlicht in: | Journal of neurochemistry 1995-10, Vol.65 (4), p.1780-1788 |
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| container_issue | 4 |
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| container_title | Journal of neurochemistry |
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| creator | Hirata, Yoko Whalin, Michael Ginty, David D. Xing, Jun Greenberg, Michael E. Milbrandt, Jeffrey Guroff, Gordon |
| description | : Nerve growth factor (NGF) induces the synthesis and the phosphorylation of the orphan nuclear receptor NGFI‐B in PC12 cells. Previous work has shown that phosphorylation, by protein kinase A, of a specific serine in the DNA‐binding domain inhibits its binding to the NGFI‐B response element. Also, cytoplasmic extracts from PC12 cells phosphorylate this serine, and phosphorylation is greater in extracts from cells treated with NGF. The present work describes the induction, identification, and partial purification of a kinase (termed NGFI‐B kinase I) from PC12 cell extracts that catalyzes this phosphorylation. Phosphorylation of the DNA‐binding domain with this purified preparation inhibits its binding to the NGFI‐B response element. The kinase is rapidly activated by treatment of the cells with NGF, and the activation lasts for at least several hours. It also is activated by fibroblast growth factor and epidermal growth factor (EGF), but the activation by EGF is quite transient. The kinase requires Mg2+ but will use Mn2+. The molecular mass of the kinase is 95–100 kDa, and it is different from protein kinase A, Fos kinase, or pp90rsk. Comparison with a partially purified preparation of cyclic AMP response element‐binding protein kinase, however, indicates that the two are either very similar or identical. |
| doi_str_mv | 10.1046/j.1471-4159.1995.65041780.x |
| format | Article |
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Previous work has shown that phosphorylation, by protein kinase A, of a specific serine in the DNA‐binding domain inhibits its binding to the NGFI‐B response element. Also, cytoplasmic extracts from PC12 cells phosphorylate this serine, and phosphorylation is greater in extracts from cells treated with NGF. The present work describes the induction, identification, and partial purification of a kinase (termed NGFI‐B kinase I) from PC12 cell extracts that catalyzes this phosphorylation. Phosphorylation of the DNA‐binding domain with this purified preparation inhibits its binding to the NGFI‐B response element. The kinase is rapidly activated by treatment of the cells with NGF, and the activation lasts for at least several hours. It also is activated by fibroblast growth factor and epidermal growth factor (EGF), but the activation by EGF is quite transient. The kinase requires Mg2+ but will use Mn2+. The molecular mass of the kinase is 95–100 kDa, and it is different from protein kinase A, Fos kinase, or pp90rsk. Comparison with a partially purified preparation of cyclic AMP response element‐binding protein kinase, however, indicates that the two are either very similar or identical.</description><identifier>ISSN: 0022-3042</identifier><identifier>EISSN: 1471-4159</identifier><identifier>DOI: 10.1046/j.1471-4159.1995.65041780.x</identifier><identifier>PMID: 7561876</identifier><identifier>CODEN: JONRA9</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Animals ; Base Sequence ; Biological and medical sciences ; Cell receptors ; Cell structures and functions ; Cyclic AMP Response Element-Binding Protein - metabolism ; DNA - metabolism ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - metabolism ; Enzyme Induction ; Epidermal Growth Factor - pharmacology ; Fibroblast Growth Factors - pharmacology ; Fundamental and applied biological sciences. Psychology ; Hormone receptors. Growth factor receptors. Cytokine receptors. 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Previous work has shown that phosphorylation, by protein kinase A, of a specific serine in the DNA‐binding domain inhibits its binding to the NGFI‐B response element. Also, cytoplasmic extracts from PC12 cells phosphorylate this serine, and phosphorylation is greater in extracts from cells treated with NGF. The present work describes the induction, identification, and partial purification of a kinase (termed NGFI‐B kinase I) from PC12 cell extracts that catalyzes this phosphorylation. Phosphorylation of the DNA‐binding domain with this purified preparation inhibits its binding to the NGFI‐B response element. The kinase is rapidly activated by treatment of the cells with NGF, and the activation lasts for at least several hours. It also is activated by fibroblast growth factor and epidermal growth factor (EGF), but the activation by EGF is quite transient. The kinase requires Mg2+ but will use Mn2+. The molecular mass of the kinase is 95–100 kDa, and it is different from protein kinase A, Fos kinase, or pp90rsk. Comparison with a partially purified preparation of cyclic AMP response element‐binding protein kinase, however, indicates that the two are either very similar or identical.</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cell receptors</subject><subject>Cell structures and functions</subject><subject>Cyclic AMP Response Element-Binding Protein - metabolism</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Enzyme Induction</subject><subject>Epidermal Growth Factor - pharmacology</subject><subject>Fibroblast Growth Factors - pharmacology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hormone receptors. Growth factor receptors. 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Prostaglandin receptors</subject><subject>Kinase</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Nerve growth factor</subject><subject>Nerve Growth Factors - pharmacology</subject><subject>NGFI‐B</subject><subject>Nuclear Receptor Subfamily 4, Group A, Member 1</subject><subject>Oligonucleotide Probes - genetics</subject><subject>PC12 Cells</subject><subject>Phosphorylation</subject><subject>Phosphotransferases - chemistry</subject><subject>Phosphotransferases - metabolism</subject><subject>Rats</subject><subject>Receptors, Cytoplasmic and Nuclear</subject><subject>Receptors, Steroid</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><issn>0022-3042</issn><issn>1471-4159</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqVkcuO0zAUhiMEGsrAIyBZArFLsBPfIlZDS0th1EFc1taJYxNXaRLshJnuZj0rnpEnIaGdbhEry_6__xxLXxS9IDghmPLX24RQQWJKWJ6QPGcJZ5gSIXFy8yCanbKH0QzjNI0zTNPH0ZMQthgTTjk5i84E40QKPovu1k056N61DWotArQx_qdBK99e9xVagu5b__v21xfTBNe7MfnoGggG9RX06FPVhq5q_b6G3oTxzaDF5mLE37qmdM13tGh34P4OnrIr31XQoM2gawMefTbadON4tFkt11PpafTIQh3Ms-N5Hn1bvvs6fx9fXq3W84vLWNNM4BgYoZoXWBtLiBZWMlNaBrkowRaC2RQKJkpZCpBlmXErJAViocBckiJP0-w8enWY2_n2x2BCr3YuaFPX0Jh2CEoIRglOxT9BwqVMpaQj-OYAat-G4I1VnXc78HtFsJqUqa2atKhJi5qUqXtl6mZsPz-uGYqdKU_do6Mxf3nMIWiorYdGu3DCMi5ShvMRWxywa1eb_f_8QH3YzO9v2R-uSreB</recordid><startdate>199510</startdate><enddate>199510</enddate><creator>Hirata, Yoko</creator><creator>Whalin, Michael</creator><creator>Ginty, David D.</creator><creator>Xing, Jun</creator><creator>Greenberg, Michael E.</creator><creator>Milbrandt, Jeffrey</creator><creator>Guroff, Gordon</creator><general>Blackwell Science Ltd</general><general>Blackwell</general><scope>IQODW</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>199510</creationdate><title>Induction of a Nerve Growth Factor‐Sensitive Kinase that Phosphorylates the DNA‐Binding Domain of the Orphan Nuclear Receptor NGFI‐B</title><author>Hirata, Yoko ; Whalin, Michael ; Ginty, David D. ; Xing, Jun ; Greenberg, Michael E. ; Milbrandt, Jeffrey ; Guroff, Gordon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4370-a514c6b0cef11c7f85edf5a97dafb75f2ab57d8d7a8dd36f784a1fab0681b9223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cell receptors</topic><topic>Cell structures and functions</topic><topic>Cyclic AMP Response Element-Binding Protein - metabolism</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Enzyme Induction</topic><topic>Epidermal Growth Factor - pharmacology</topic><topic>Fibroblast Growth Factors - pharmacology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors</topic><topic>Kinase</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Nerve growth factor</topic><topic>Nerve Growth Factors - pharmacology</topic><topic>NGFI‐B</topic><topic>Nuclear Receptor Subfamily 4, Group A, Member 1</topic><topic>Oligonucleotide Probes - genetics</topic><topic>PC12 Cells</topic><topic>Phosphorylation</topic><topic>Phosphotransferases - chemistry</topic><topic>Phosphotransferases - metabolism</topic><topic>Rats</topic><topic>Receptors, Cytoplasmic and Nuclear</topic><topic>Receptors, Steroid</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirata, Yoko</creatorcontrib><creatorcontrib>Whalin, Michael</creatorcontrib><creatorcontrib>Ginty, David D.</creatorcontrib><creatorcontrib>Xing, Jun</creatorcontrib><creatorcontrib>Greenberg, Michael E.</creatorcontrib><creatorcontrib>Milbrandt, Jeffrey</creatorcontrib><creatorcontrib>Guroff, Gordon</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of neurochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirata, Yoko</au><au>Whalin, Michael</au><au>Ginty, David D.</au><au>Xing, Jun</au><au>Greenberg, Michael E.</au><au>Milbrandt, Jeffrey</au><au>Guroff, Gordon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Induction of a Nerve Growth Factor‐Sensitive Kinase that Phosphorylates the DNA‐Binding Domain of the Orphan Nuclear Receptor NGFI‐B</atitle><jtitle>Journal of neurochemistry</jtitle><addtitle>J Neurochem</addtitle><date>1995-10</date><risdate>1995</risdate><volume>65</volume><issue>4</issue><spage>1780</spage><epage>1788</epage><pages>1780-1788</pages><issn>0022-3042</issn><eissn>1471-4159</eissn><coden>JONRA9</coden><abstract>: Nerve growth factor (NGF) induces the synthesis and the phosphorylation of the orphan nuclear receptor NGFI‐B in PC12 cells. Previous work has shown that phosphorylation, by protein kinase A, of a specific serine in the DNA‐binding domain inhibits its binding to the NGFI‐B response element. Also, cytoplasmic extracts from PC12 cells phosphorylate this serine, and phosphorylation is greater in extracts from cells treated with NGF. The present work describes the induction, identification, and partial purification of a kinase (termed NGFI‐B kinase I) from PC12 cell extracts that catalyzes this phosphorylation. Phosphorylation of the DNA‐binding domain with this purified preparation inhibits its binding to the NGFI‐B response element. The kinase is rapidly activated by treatment of the cells with NGF, and the activation lasts for at least several hours. It also is activated by fibroblast growth factor and epidermal growth factor (EGF), but the activation by EGF is quite transient. The kinase requires Mg2+ but will use Mn2+. The molecular mass of the kinase is 95–100 kDa, and it is different from protein kinase A, Fos kinase, or pp90rsk. Comparison with a partially purified preparation of cyclic AMP response element‐binding protein kinase, however, indicates that the two are either very similar or identical.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>7561876</pmid><doi>10.1046/j.1471-4159.1995.65041780.x</doi><tpages>9</tpages></addata></record> |
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| ispartof | Journal of neurochemistry, 1995-10, Vol.65 (4), p.1780-1788 |
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| source | MEDLINE; Wiley Journals |
| subjects | Animals Base Sequence Biological and medical sciences Cell receptors Cell structures and functions Cyclic AMP Response Element-Binding Protein - metabolism DNA - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Enzyme Induction Epidermal Growth Factor - pharmacology Fibroblast Growth Factors - pharmacology Fundamental and applied biological sciences. Psychology Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors Kinase Molecular and cellular biology Molecular Sequence Data Molecular Weight Nerve growth factor Nerve Growth Factors - pharmacology NGFI‐B Nuclear Receptor Subfamily 4, Group A, Member 1 Oligonucleotide Probes - genetics PC12 Cells Phosphorylation Phosphotransferases - chemistry Phosphotransferases - metabolism Rats Receptors, Cytoplasmic and Nuclear Receptors, Steroid Transcription Factors - chemistry Transcription Factors - metabolism |
| title | Induction of a Nerve Growth Factor‐Sensitive Kinase that Phosphorylates the DNA‐Binding Domain of the Orphan Nuclear Receptor NGFI‐B |
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