Publikation: The sterile alpha-motif (SAM) domain of p63 binds in vitro monoasialoganglioside (GM1) micelles
Dateien
Datum
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Publikationsstatus
Erschienen in
Zusammenfassung
The transcription factor p63 plays pivotal roles in epidermal barrier formation and in embryonic development. The protein structures of TAp63 and ΔNp63α isoforms include a C-terminal steril alpha-motif (SAM) involved in protein-protein interaction. Identification of p63 SAM domain interactors could lead to the explanation of novel mechanisms of regulation of p63 activity, possibly relevant in the physiological role of p63 and in genetic disorders associated with mutations of the p63 gene. In this work, we have performed a biochemical analysis of p63 SAM domain preferences in lipid binding. We have identified the ganglioside GM1 as a high affinity interactor, capable of modulating p63 transcriptional ability exclusively on epidermal target genes. In agreement with these data we report a consistent expression profile and localization analysis of p63 and GM1 in primary keratinocytes and in human epidermal biopsies. Therefore, we propose a potential biological role of p63-GM1 interaction in regulation of p63 during epidermal differentiation.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
Schlagwörter
Konferenz
Rezension
Zitieren
ISO 690
RUFINI, Stefano, Anna Maria LENA, Bruno CADOT, Sonia MELE, Ivano AMELIO, Alessandro TERRINONI, Alessandro DESIDERI, Gerry MELINO, Eleonora CANDI, 2011. The sterile alpha-motif (SAM) domain of p63 binds in vitro monoasialoganglioside (GM1) micelles. In: Biochemical Pharmacology. Elsevier. 2011, 82(10), pp. 1262-1268. ISSN 0006-2952. eISSN 1873-2968. Available under: doi: 10.1016/j.bcp.2011.07.087BibTex
@article{Rufini2011-11-15steri-56893, year={2011}, doi={10.1016/j.bcp.2011.07.087}, title={The sterile alpha-motif (SAM) domain of p63 binds in vitro monoasialoganglioside (GM1) micelles}, number={10}, volume={82}, issn={0006-2952}, journal={Biochemical Pharmacology}, pages={1262--1268}, author={Rufini, Stefano and Lena, Anna Maria and Cadot, Bruno and Mele, Sonia and Amelio, Ivano and Terrinoni, Alessandro and Desideri, Alessandro and Melino, Gerry and Candi, Eleonora} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/56893"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-03-16T14:25:14Z</dc:date> <dc:contributor>Amelio, Ivano</dc:contributor> <dc:creator>Melino, Gerry</dc:creator> <dcterms:abstract xml:lang="eng">The transcription factor p63 plays pivotal roles in epidermal barrier formation and in embryonic development. The protein structures of TAp63 and ΔNp63α isoforms include a C-terminal steril alpha-motif (SAM) involved in protein-protein interaction. Identification of p63 SAM domain interactors could lead to the explanation of novel mechanisms of regulation of p63 activity, possibly relevant in the physiological role of p63 and in genetic disorders associated with mutations of the p63 gene. In this work, we have performed a biochemical analysis of p63 SAM domain preferences in lipid binding. We have identified the ganglioside GM1 as a high affinity interactor, capable of modulating p63 transcriptional ability exclusively on epidermal target genes. In agreement with these data we report a consistent expression profile and localization analysis of p63 and GM1 in primary keratinocytes and in human epidermal biopsies. Therefore, we propose a potential biological role of p63-GM1 interaction in regulation of p63 during epidermal differentiation.</dcterms:abstract> <dcterms:title>The sterile alpha-motif (SAM) domain of p63 binds in vitro monoasialoganglioside (GM1) micelles</dcterms:title> <dc:language>eng</dc:language> <dc:contributor>Rufini, Stefano</dc:contributor> <dc:contributor>Lena, Anna Maria</dc:contributor> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <dcterms:rights rdf:resource="https://rightsstatements.org/page/InC/1.0/"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:contributor>Terrinoni, Alessandro</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2022-03-16T14:25:14Z</dcterms:available> <dc:rights>terms-of-use</dc:rights> <dc:creator>Cadot, Bruno</dc:creator> <dc:creator>Lena, Anna Maria</dc:creator> <dc:creator>Terrinoni, Alessandro</dc:creator> <dc:contributor>Candi, Eleonora</dc:contributor> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/28"/> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/56893"/> <dc:creator>Candi, Eleonora</dc:creator> <dc:contributor>Melino, Gerry</dc:contributor> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dc:contributor>Mele, Sonia</dc:contributor> <dc:creator>Amelio, Ivano</dc:creator> <dc:contributor>Cadot, Bruno</dc:contributor> <dc:contributor>Desideri, Alessandro</dc:contributor> <dc:creator>Mele, Sonia</dc:creator> <dc:creator>Desideri, Alessandro</dc:creator> <dc:creator>Rufini, Stefano</dc:creator> <dcterms:issued>2011-11-15</dcterms:issued> </rdf:Description> </rdf:RDF>