PubMed:8663380 JSONTXT

{"project":"CL-cell","denotations":[{"id":"T1","span":{"begin":10,"end":15},"obj":"Cell"},{"id":"T2","span":{"begin":231,"end":236},"obj":"Cell"},{"id":"T3","span":{"begin":459,"end":478},"obj":"Cell"},{"id":"T4","span":{"begin":679,"end":684},"obj":"Cell"},{"id":"T5","span":{"begin":1211,"end":1216},"obj":"Cell"},{"id":"T6","span":{"begin":1357,"end":1362},"obj":"Cell"}],"attributes":[{"id":"A1","pred":"cl_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A2","pred":"cl_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A3","pred":"cl_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/CL:0000293"},{"id":"A4","pred":"cl_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A5","pred":"cl_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/CL:0004124"},{"id":"A6","pred":"cl_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/CL:0004124"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":271},"obj":"Sentence"},{"id":"T3","span":{"begin":272,"end":426},"obj":"Sentence"},{"id":"T4","span":{"begin":427,"end":692},"obj":"Sentence"},{"id":"T5","span":{"begin":693,"end":873},"obj":"Sentence"},{"id":"T6","span":{"begin":874,"end":1029},"obj":"Sentence"},{"id":"T7","span":{"begin":1030,"end":1111},"obj":"Sentence"},{"id":"T8","span":{"begin":1112,"end":1376},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"T2","span":{"begin":115,"end":271},"obj":"Sentence"},{"id":"T3","span":{"begin":272,"end":426},"obj":"Sentence"},{"id":"T4","span":{"begin":427,"end":692},"obj":"Sentence"},{"id":"T5","span":{"begin":693,"end":873},"obj":"Sentence"},{"id":"T6","span":{"begin":874,"end":1029},"obj":"Sentence"},{"id":"T7","span":{"begin":1030,"end":1111},"obj":"Sentence"},{"id":"T8","span":{"begin":1112,"end":1376},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":97},"obj":"http://purl.obolibrary.org/obo/MAT_0000077"},{"id":"T2","span":{"begin":637,"end":646},"obj":"http://purl.obolibrary.org/obo/MAT_0000077"},{"id":"T3","span":{"begin":955,"end":963},"obj":"http://purl.obolibrary.org/obo/MAT_0000491"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"jnlpba-st-training","denotations":[{"id":"T1","span":{"begin":4,"end":22},"obj":"protein"},{"id":"T2","span":{"begin":32,"end":55},"obj":"DNA"},{"id":"T3","span":{"begin":164,"end":169},"obj":"protein"},{"id":"T4","span":{"begin":187,"end":217},"obj":"protein"},{"id":"T5","span":{"begin":231,"end":243},"obj":"protein"},{"id":"T6","span":{"begin":265,"end":270},"obj":"protein"},{"id":"T7","span":{"begin":302,"end":307},"obj":"protein"},{"id":"T8","span":{"begin":337,"end":366},"obj":"DNA"},{"id":"T9","span":{"begin":394,"end":407},"obj":"protein"},{"id":"T10","span":{"begin":510,"end":515},"obj":"protein"},{"id":"T11","span":{"begin":559,"end":564},"obj":"protein"},{"id":"T12","span":{"begin":599,"end":631},"obj":"DNA"},{"id":"T13","span":{"begin":673,"end":691},"obj":"protein"},{"id":"T14","span":{"begin":750,"end":761},"obj":"DNA"},{"id":"T15","span":{"begin":763,"end":775},"obj":"DNA"},{"id":"T16","span":{"begin":815,"end":820},"obj":"protein"},{"id":"T17","span":{"begin":826,"end":851},"obj":"protein"},{"id":"T18","span":{"begin":859,"end":872},"obj":"DNA"},{"id":"T19","span":{"begin":877,"end":900},"obj":"cell_line"},{"id":"T20","span":{"begin":902,"end":907},"obj":"protein"},{"id":"T21","span":{"begin":928,"end":941},"obj":"DNA"},{"id":"T22","span":{"begin":964,"end":988},"obj":"DNA"},{"id":"T23","span":{"begin":990,"end":1001},"obj":"DNA"},{"id":"T24","span":{"begin":1023,"end":1028},"obj":"protein"},{"id":"T25","span":{"begin":1051,"end":1056},"obj":"protein"},{"id":"T26","span":{"begin":1082,"end":1087},"obj":"protein"},{"id":"T27","span":{"begin":1096,"end":1110},"obj":"protein"},{"id":"T28","span":{"begin":1205,"end":1223},"obj":"protein"},{"id":"T29","span":{"begin":1303,"end":1308},"obj":"protein"},{"id":"T30","span":{"begin":1357,"end":1375},"obj":"protein"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":114},"obj":"Sentence"},{"id":"S2","span":{"begin":115,"end":271},"obj":"Sentence"},{"id":"S3","span":{"begin":272,"end":426},"obj":"Sentence"},{"id":"S4","span":{"begin":427,"end":692},"obj":"Sentence"},{"id":"S5","span":{"begin":693,"end":873},"obj":"Sentence"},{"id":"S6","span":{"begin":874,"end":1029},"obj":"Sentence"},{"id":"S7","span":{"begin":1030,"end":1111},"obj":"Sentence"},{"id":"S8","span":{"begin":1112,"end":1376},"obj":"Sentence"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"genia-medco-coref","denotations":[{"id":"C7","span":{"begin":0,"end":22},"obj":"NP"},{"id":"C1","span":{"begin":164,"end":169},"obj":"NP"},{"id":"C10","span":{"begin":185,"end":217},"obj":"NP"},{"id":"C9","span":{"begin":227,"end":243},"obj":"NP"},{"id":"C3","span":{"begin":245,"end":250},"obj":"NP"},{"id":"C4","span":{"begin":302,"end":307},"obj":"NP"},{"id":"C5","span":{"begin":505,"end":535},"obj":"NP"},{"id":"C6","span":{"begin":554,"end":584},"obj":"NP"},{"id":"C8","span":{"begin":669,"end":691},"obj":"NP"},{"id":"C11","span":{"begin":815,"end":820},"obj":"NP"},{"id":"C13","span":{"begin":855,"end":872},"obj":"NP"},{"id":"C12","span":{"begin":902,"end":907},"obj":"NP"},{"id":"C14","span":{"begin":924,"end":941},"obj":"NP"},{"id":"C15","span":{"begin":1082,"end":1087},"obj":"NP"},{"id":"C16","span":{"begin":1167,"end":1191},"obj":"NP"},{"id":"C17","span":{"begin":1195,"end":1200},"obj":"NP"},{"id":"C18","span":{"begin":1201,"end":1223},"obj":"NP"},{"id":"C19","span":{"begin":1303,"end":1308},"obj":"NP"},{"id":"C20","span":{"begin":1353,"end":1375},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C9","obj":"C10"},{"id":"R2","pred":"coref-relat","subj":"C3","obj":"C10"},{"id":"R3","pred":"coref-ident","subj":"C4","obj":"C1"},{"id":"R4","pred":"coref-ident","subj":"C6","obj":"C5"},{"id":"R5","pred":"coref-ident","subj":"C8","obj":"C7"},{"id":"R6","pred":"coref-ident","subj":"C11","obj":"C4"},{"id":"R7","pred":"coref-ident","subj":"C12","obj":"C11"},{"id":"R8","pred":"coref-ident","subj":"C14","obj":"C13"},{"id":"R9","pred":"coref-ident","subj":"C15","obj":"C12"},{"id":"R10","pred":"coref-relat","subj":"C17","obj":"C16"},{"id":"R11","pred":"coref-ident","subj":"C18","obj":"C8"},{"id":"R12","pred":"coref-ident","subj":"C19","obj":"C15"},{"id":"R13","pred":"coref-ident","subj":"C20","obj":"C10"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"GENIAcorpus","denotations":[{"id":"T1","span":{"begin":4,"end":9},"obj":"protein_molecule"},{"id":"T2","span":{"begin":32,"end":55},"obj":"DNA_domain_or_region"},{"id":"T3","span":{"begin":119,"end":160},"obj":"other_name"},{"id":"T4","span":{"begin":164,"end":169},"obj":"protein_molecule"},{"id":"T5","span":{"begin":187,"end":217},"obj":"protein_domain_or_region"},{"id":"T6","span":{"begin":231,"end":243},"obj":"protein_domain_or_region"},{"id":"T7","span":{"begin":265,"end":270},"obj":"protein_molecule"},{"id":"T8","span":{"begin":302,"end":307},"obj":"protein_molecule"},{"id":"T9","span":{"begin":337,"end":366},"obj":"DNA_domain_or_region"},{"id":"T10","span":{"begin":394,"end":407},"obj":"protein_molecule"},{"id":"T11","span":{"begin":411,"end":425},"obj":"other_organic_compound"},{"id":"T12","span":{"begin":474,"end":500},"obj":"other_name"},{"id":"T13","span":{"begin":510,"end":515},"obj":"protein_molecule"},{"id":"T14","span":{"begin":559,"end":564},"obj":"protein_molecule"},{"id":"T15","span":{"begin":599,"end":631},"obj":"DNA_domain_or_region"},{"id":"T16","span":{"begin":673,"end":678},"obj":"protein_molecule"},{"id":"T17","span":{"begin":750,"end":761},"obj":"DNA_family_or_group"},{"id":"T18","span":{"begin":763,"end":775},"obj":"DNA_family_or_group"},{"id":"T19","span":{"begin":780,"end":804},"obj":"other_name"},{"id":"T20","span":{"begin":815,"end":820},"obj":"protein_molecule"},{"id":"T21","span":{"begin":826,"end":851},"obj":"protein_family_or_group"},{"id":"T22","span":{"begin":859,"end":872},"obj":"DNA_domain_or_region"},{"id":"T23","span":{"begin":877,"end":900},"obj":"cell_line"},{"id":"T24","span":{"begin":902,"end":907},"obj":"protein_molecule"},{"id":"T25","span":{"begin":928,"end":941},"obj":"DNA_domain_or_region"},{"id":"T26","span":{"begin":964,"end":988},"obj":"DNA_domain_or_region"},{"id":"T27","span":{"begin":990,"end":1001},"obj":"DNA_domain_or_region"},{"id":"T28","span":{"begin":1023,"end":1028},"obj":"protein_molecule"},{"id":"T29","span":{"begin":1051,"end":1056},"obj":"protein_molecule"},{"id":"T30","span":{"begin":1082,"end":1087},"obj":"protein_molecule"},{"id":"T31","span":{"begin":1096,"end":1110},"obj":"protein_molecule"},{"id":"T32","span":{"begin":1205,"end":1210},"obj":"protein_molecule"},{"id":"T33","span":{"begin":1239,"end":1256},"obj":"other_name"},{"id":"T34","span":{"begin":1303,"end":1308},"obj":"protein_molecule"},{"id":"T35","span":{"begin":1357,"end":1375},"obj":"protein_domain_or_region"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":88,"end":97},"obj":"Disease"},{"id":"T2","span":{"begin":637,"end":646},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0021156"},{"id":"A2","pred":"mondo_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MONDO_0021156"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":337,"end":340},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"10114"},{"id":"A2","pred":"db_id","subj":"T1","obj":"10116"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":88,"end":97},"obj":"Body_part"},{"id":"T2","span":{"begin":637,"end":646},"obj":"Body_part"},{"id":"T3","span":{"begin":955,"end":963},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000077"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000077"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000491"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":88,"end":97},"obj":"Body_part"},{"id":"T2","span":{"begin":459,"end":478},"obj":"Body_part"},{"id":"T3","span":{"begin":637,"end":646},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000007"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/CL_0000293"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0000007"}],"text":"The c-Jun delta-domain inhibits neuroendocrine promoter activity in a DNA sequence- and pituitary-specific manner.\nThe transcription and transformation activity of c-Jun is governed by a 27-amino acid regulatory motif, labeled the delta-domain, which is deleted in v-Jun. We have previously shown that c-Jun is a potent inhibitor of the rat prolactin (rPRL) promoter activity induced by either oncogenic Ras or phorbol esters. Here, we have characterized the structural and cell-specific requirements for this c-Jun inhibitory response, and we show that this c-Jun inhibitory response mapped to the rPRL footprint II repressor site, was pituitary-specific and required the c-Jun delta-domain. Moreover, alteration of any one of these features (e.g., cis-element, trans-factor, or cell-specific background) switched c-Jun to a transcriptional activator of the rPRL promoter. In HeLa nonpituitary cells, c-Jun alone activated the rPRL promoter via the most proximal GHF-1/Pit-1 binding site, footprint I, and synergized with GHF-1. Finally, recombinant GHF-1 interacted directly with c-Jun but not c-Fos proteins. These data provide important fundamental insights into the molecular mechanisms by which the c-Jun delta-domain functions as a modulatory switch and further imply that the functional role of c-Jun is dictated by cell-specific influences and the delta-domain motif."}