PubMed:18356166 JSONTXT

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":417,"end":420},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":628,"end":631},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":765,"end":768},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":848,"end":851},"obj":"Glycan_Motif"},{"id":"T5","span":{"begin":889,"end":892},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00063MO"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00063MO"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00063MO"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00063MO"},{"id":"A5","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G00063MO"}],"text":"A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.\nCell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by gamma-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus."}

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":898,"end":901},"obj":"DiseaseOrPhenotypicFeature"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"0012833"}],"text":"A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.\nCell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by gamma-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus."}

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":71},"obj":"Sentence"},{"id":"T2","span":{"begin":72,"end":224},"obj":"Sentence"},{"id":"T3","span":{"begin":225,"end":331},"obj":"Sentence"},{"id":"T4","span":{"begin":332,"end":445},"obj":"Sentence"},{"id":"T5","span":{"begin":446,"end":500},"obj":"Sentence"},{"id":"T6","span":{"begin":501,"end":637},"obj":"Sentence"},{"id":"T7","span":{"begin":638,"end":774},"obj":"Sentence"},{"id":"T8","span":{"begin":775,"end":864},"obj":"Sentence"},{"id":"T9","span":{"begin":865,"end":968},"obj":"Sentence"},{"id":"T10","span":{"begin":969,"end":1040},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":71},"obj":"Sentence"},{"id":"T2","span":{"begin":72,"end":224},"obj":"Sentence"},{"id":"T3","span":{"begin":225,"end":331},"obj":"Sentence"},{"id":"T4","span":{"begin":332,"end":445},"obj":"Sentence"},{"id":"T5","span":{"begin":446,"end":500},"obj":"Sentence"},{"id":"T6","span":{"begin":501,"end":637},"obj":"Sentence"},{"id":"T7","span":{"begin":638,"end":774},"obj":"Sentence"},{"id":"T8","span":{"begin":775,"end":864},"obj":"Sentence"},{"id":"T9","span":{"begin":865,"end":968},"obj":"Sentence"},{"id":"T10","span":{"begin":969,"end":1040},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.\nCell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by gamma-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus."}

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":417,"end":420},"obj":"https://glytoucan.org/Structures/Glycans/G00063MO"},{"id":"T2","span":{"begin":628,"end":631},"obj":"https://glytoucan.org/Structures/Glycans/G00063MO"},{"id":"T3","span":{"begin":765,"end":768},"obj":"https://glytoucan.org/Structures/Glycans/G00063MO"},{"id":"T4","span":{"begin":848,"end":851},"obj":"https://glytoucan.org/Structures/Glycans/G00063MO"},{"id":"T5","span":{"begin":889,"end":892},"obj":"https://glytoucan.org/Structures/Glycans/G00063MO"}],"text":"A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.\nCell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by gamma-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":23,"end":34},"obj":"Body_part"},{"id":"T2","span":{"begin":63,"end":70},"obj":"Body_part"},{"id":"T4","span":{"begin":112,"end":125},"obj":"Body_part"},{"id":"T5","span":{"begin":437,"end":444},"obj":"Body_part"},{"id":"T6","span":{"begin":960,"end":967},"obj":"Body_part"},{"id":"T8","span":{"begin":1032,"end":1039},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0005737"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/GO_0005634"},{"id":"A3","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0000125"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/GO_0005622"},{"id":"A5","pred":"uberon_id","subj":"T5","obj":"http://purl.obolibrary.org/obo/GO_0005829"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/GO_0005634"},{"id":"A7","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0000125"},{"id":"A8","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/GO_0005634"},{"id":"A9","pred":"uberon_id","subj":"T8","obj":"http://purl.obolibrary.org/obo/UBERON_0000125"}],"text":"A role for the cleaved cytoplasmic domain of E-cadherin in the nucleus.\nCell-cell contacts play a vital role in intracellular signaling, although the molecular mechanisms of these signaling pathways are not fully understood. E-cadherin, an important mediator of cell-cell adhesions, has been shown to be cleaved by gamma-secretase. This cleavage releases a fragment of E-cadherin, E-cadherin C-terminal fragment 2 (E-cad/CTF2), into the cytosol. Here, we study the fate and function of this fragment. First, we show that coexpression of the cadherin-binding protein, p120 catenin (p120), enhances the nuclear translocation of E-cad/CTF2. By knocking down p120 with short interfering RNA, we also demonstrate that p120 is necessary for the nuclear localization of E-cad/CTF2. Furthermore, p120 enhances and is required for the specific binding of E-cad/CTF2 to DNA. Finally, we show that E-cad/CTF2 can regulate the p120-Kaiso-mediated signaling pathway in the nucleus. These data indicate a novel role for cleaved E-cadherin in the nucleus."}