The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription
Teneurin-2, a vertebrate homologue of the Drosophila pair-rule gene ten-m/odz, is revealed to be a membrane-bound transcription regulator. In the nucleus, the intracellular domain of teneurin-2 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies implicated in transcription contro...
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| Veröffentlicht in: | Journal of cell science 2003-07, Vol.116 (Pt 14), p.2957-2966 |
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| container_issue | Pt 14 |
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| container_title | Journal of cell science |
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| creator | Bagutti, Claudia Forro, Gaby Ferralli, Jacqueline Rubin, Beatrix Chiquet-Ehrismann, Ruth |
| description | Teneurin-2, a vertebrate homologue of the Drosophila pair-rule gene ten-m/odz, is revealed to be a membrane-bound transcription regulator. In the nucleus, the intracellular domain of teneurin-2 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies implicated in transcription control. Since Drosophila ten-m acts epistatically to another pair-rule gene opa, we investigated whether gene regulation by the mammalian opa homologue zic-1 was influenced by the intracellular domain of teneurin-2. We found that zic-mediated transcription from the apolipoprotein E promoter was inhibited. Release of the intracellular domain of teneurin-2 could be stimulated by homophilic interaction of the extracellular domain, and the intracellular domain was stabilized by proteasome inhibitors. We have previously shown that teneurin-2 is expressed by neurons belonging to the same functional circuit. Therefore, we hypothesize that homophilic interaction enables neurons to identify their targets and that the release of the intracellular domain of teneurin-2 provides them with a signal to switch their gene expression program from growth towards differentiation once the proper contact has been made. |
| doi_str_mv | 10.1242/jcs.00603 |
| format | Article |
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In the nucleus, the intracellular domain of teneurin-2 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies implicated in transcription control. Since Drosophila ten-m acts epistatically to another pair-rule gene opa, we investigated whether gene regulation by the mammalian opa homologue zic-1 was influenced by the intracellular domain of teneurin-2. We found that zic-mediated transcription from the apolipoprotein E promoter was inhibited. Release of the intracellular domain of teneurin-2 could be stimulated by homophilic interaction of the extracellular domain, and the intracellular domain was stabilized by proteasome inhibitors. We have previously shown that teneurin-2 is expressed by neurons belonging to the same functional circuit. 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In the nucleus, the intracellular domain of teneurin-2 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies implicated in transcription control. Since Drosophila ten-m acts epistatically to another pair-rule gene opa, we investigated whether gene regulation by the mammalian opa homologue zic-1 was influenced by the intracellular domain of teneurin-2. We found that zic-mediated transcription from the apolipoprotein E promoter was inhibited. Release of the intracellular domain of teneurin-2 could be stimulated by homophilic interaction of the extracellular domain, and the intracellular domain was stabilized by proteasome inhibitors. We have previously shown that teneurin-2 is expressed by neurons belonging to the same functional circuit. Therefore, we hypothesize that homophilic interaction enables neurons to identify their targets and that the release of the intracellular domain of teneurin-2 provides them with a signal to switch their gene expression program from growth towards differentiation once the proper contact has been made.</description><subject>Acetylcysteine - analogs & derivatives</subject><subject>Acetylcysteine - pharmacology</subject><subject>Animals</subject><subject>Apolipoproteins E - genetics</subject><subject>Avian Proteins - chemistry</subject><subject>Avian Proteins - physiology</subject><subject>beta-Galactosidase - metabolism</subject><subject>Blotting, Western</subject><subject>Cell Differentiation</subject><subject>Cell Line</subject><subject>Cell Line, Tumor</subject><subject>Cell Membrane - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>COS Cells</subject><subject>Cysteine Endopeptidases</subject><subject>Dose-Response Relationship, Drug</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Luciferases - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - physiology</subject><subject>Microscopy, Fluorescence</subject><subject>Models, Biological</subject><subject>Multienzyme Complexes - antagonists & inhibitors</subject><subject>Neoplasm Proteins - metabolism</subject><subject>Nerve Tissue Proteins - chemistry</subject><subject>Nerve Tissue Proteins - physiology</subject><subject>Nuclear Proteins</subject><subject>Promoter Regions, Genetic</subject><subject>Promyelocytic Leukemia Protein</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Signal Transduction</subject><subject>Time Factors</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription, Genetic</subject><subject>Transfection</subject><subject>Tumor Suppressor Proteins</subject><issn>0021-9533</issn><issn>1477-9137</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkDtPwzAURi0EoqUw8AeQJyQGF78SxyOqeEmVWMocOc6N6ipxgp0M8OtxaCWmuxwd3e8gdMvomnHJHw82rinNqThDSyaVIpoJdY6WlHJGdCbEAl3FeKCUKq7VJVowrgqhNV2i_W4P2PkxGAttO7Um4LrvjPO4b_AIHqbgPOF4byI22E-2hYQ0k7ej6z02vsYBhgAxQsQ_zhJGOqidGaHGSeqjDW6Y0Wt00Zg2ws3prtDny_Nu80a2H6_vm6ctsaKQI-EqFzlwIdOvRkiomMhtxWwmpNLCVlBokTFNs8ZkiknN0yheZGC0pFlRK7FC90fvEPqvCeJYdi7O24yHfoqlSmrO1Qw-HEEb-hgDNOUQXGfCd8loOWctU9byL2ti707SqUrz_slTR_ELYm1yMA</recordid><startdate>20030715</startdate><enddate>20030715</enddate><creator>Bagutti, Claudia</creator><creator>Forro, Gaby</creator><creator>Ferralli, Jacqueline</creator><creator>Rubin, Beatrix</creator><creator>Chiquet-Ehrismann, Ruth</creator><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>7X8</scope></search><sort><creationdate>20030715</creationdate><title>The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription</title><author>Bagutti, Claudia ; Forro, Gaby ; Ferralli, Jacqueline ; Rubin, Beatrix ; Chiquet-Ehrismann, Ruth</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c384t-27636e234007a34eb136cb1c534793cbe89351905fa571492000285ea94058d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Acetylcysteine - analogs & derivatives</topic><topic>Acetylcysteine - pharmacology</topic><topic>Animals</topic><topic>Apolipoproteins E - genetics</topic><topic>Avian Proteins - chemistry</topic><topic>Avian Proteins - physiology</topic><topic>beta-Galactosidase - metabolism</topic><topic>Blotting, Western</topic><topic>Cell Differentiation</topic><topic>Cell Line</topic><topic>Cell Line, Tumor</topic><topic>Cell Membrane - metabolism</topic><topic>Cell Nucleus - metabolism</topic><topic>COS Cells</topic><topic>Cysteine Endopeptidases</topic><topic>Dose-Response Relationship, Drug</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Luciferases - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - physiology</topic><topic>Microscopy, Fluorescence</topic><topic>Models, Biological</topic><topic>Multienzyme Complexes - antagonists & inhibitors</topic><topic>Neoplasm Proteins - metabolism</topic><topic>Nerve Tissue Proteins - chemistry</topic><topic>Nerve Tissue Proteins - physiology</topic><topic>Nuclear Proteins</topic><topic>Promoter Regions, Genetic</topic><topic>Promyelocytic Leukemia Protein</topic><topic>Proteasome Endopeptidase Complex</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Signal Transduction</topic><topic>Time Factors</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription, Genetic</topic><topic>Transfection</topic><topic>Tumor Suppressor Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bagutti, Claudia</creatorcontrib><creatorcontrib>Forro, Gaby</creatorcontrib><creatorcontrib>Ferralli, Jacqueline</creatorcontrib><creatorcontrib>Rubin, Beatrix</creatorcontrib><creatorcontrib>Chiquet-Ehrismann, Ruth</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cell science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bagutti, Claudia</au><au>Forro, Gaby</au><au>Ferralli, Jacqueline</au><au>Rubin, Beatrix</au><au>Chiquet-Ehrismann, Ruth</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription</atitle><jtitle>Journal of cell science</jtitle><addtitle>J Cell Sci</addtitle><date>2003-07-15</date><risdate>2003</risdate><volume>116</volume><issue>Pt 14</issue><spage>2957</spage><epage>2966</epage><pages>2957-2966</pages><issn>0021-9533</issn><eissn>1477-9137</eissn><abstract>Teneurin-2, a vertebrate homologue of the Drosophila pair-rule gene ten-m/odz, is revealed to be a membrane-bound transcription regulator. In the nucleus, the intracellular domain of teneurin-2 colocalizes with promyelocytic leukemia (PML) protein in nuclear bodies implicated in transcription control. Since Drosophila ten-m acts epistatically to another pair-rule gene opa, we investigated whether gene regulation by the mammalian opa homologue zic-1 was influenced by the intracellular domain of teneurin-2. We found that zic-mediated transcription from the apolipoprotein E promoter was inhibited. Release of the intracellular domain of teneurin-2 could be stimulated by homophilic interaction of the extracellular domain, and the intracellular domain was stabilized by proteasome inhibitors. We have previously shown that teneurin-2 is expressed by neurons belonging to the same functional circuit. Therefore, we hypothesize that homophilic interaction enables neurons to identify their targets and that the release of the intracellular domain of teneurin-2 provides them with a signal to switch their gene expression program from growth towards differentiation once the proper contact has been made.</abstract><cop>England</cop><pmid>12783990</pmid><doi>10.1242/jcs.00603</doi><tpages>10</tpages></addata></record> |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Company of Biologists |
| subjects | Acetylcysteine - analogs & derivatives Acetylcysteine - pharmacology Animals Apolipoproteins E - genetics Avian Proteins - chemistry Avian Proteins - physiology beta-Galactosidase - metabolism Blotting, Western Cell Differentiation Cell Line Cell Line, Tumor Cell Membrane - metabolism Cell Nucleus - metabolism COS Cells Cysteine Endopeptidases Dose-Response Relationship, Drug Gene Expression Regulation Humans Luciferases - metabolism Membrane Proteins - chemistry Membrane Proteins - physiology Microscopy, Fluorescence Models, Biological Multienzyme Complexes - antagonists & inhibitors Neoplasm Proteins - metabolism Nerve Tissue Proteins - chemistry Nerve Tissue Proteins - physiology Nuclear Proteins Promoter Regions, Genetic Promyelocytic Leukemia Protein Proteasome Endopeptidase Complex Protein Binding Protein Structure, Tertiary Signal Transduction Time Factors Transcription Factors - metabolism Transcription, Genetic Transfection Tumor Suppressor Proteins |
| title | The intracellular domain of teneurin-2 has a nuclear function and represses zic-1-mediated transcription |
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