Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.

2.50
Hdl Handle:
http://hdl.handle.net/10541/95895
Title:
Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.
Authors:
Deed, Richard W; Armitage, Suzanne; Norton, John D
Abstract:
Members of the Id family of helix-loop-helix proteins function as negative regulators of DNA binding, E protein, helix-loop-helix transcription factors in the control of cell growth, differentiation, and development. By using transient transfection analysis of COS cells, we show that in the absence of its E protein target, the Id3 protein is localized exclusively to the cytoplasm/perinuclear region. Co-transfection with E protein (E47) results in nuclear translocation of the Id3 protein, a process requiring both a functional Id helix-loop-helix dimerization domain and an E protein nuclear localization signal. Id3 that is associated with E protein displays an extended half-life, while the E protein itself is more rapidly turned over. These observations demonstrate that E protein, by nuclear chaperoning Id, can regulate the available cellular pool of its own inhibitory partner.
Affiliation:
Cancer Research Campaign Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital National Health Service Trust, Wilmslow Road, Manchester M20 9BX, United Kingdom.
Citation:
Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. 1996, 271 (39):23603-6 J. Biol. Chem.
Journal:
The Journal of Biological Chemistry
Issue Date:
27-Sep-1996
URI:
http://hdl.handle.net/10541/95895
DOI:
10.1074/jbc.271.39.23603
PubMed ID:
8798572
Type:
Article
Language:
en
ISSN:
0021-9258
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorDeed, Richard Wen
dc.contributor.authorArmitage, Suzanneen
dc.contributor.authorNorton, John Den
dc.date.accessioned2010-04-07T13:11:35Z-
dc.date.available2010-04-07T13:11:35Z-
dc.date.issued1996-09-27-
dc.identifier.citationNuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. 1996, 271 (39):23603-6 J. Biol. Chem.en
dc.identifier.issn0021-9258-
dc.identifier.pmid8798572-
dc.identifier.doi10.1074/jbc.271.39.23603-
dc.identifier.urihttp://hdl.handle.net/10541/95895-
dc.description.abstractMembers of the Id family of helix-loop-helix proteins function as negative regulators of DNA binding, E protein, helix-loop-helix transcription factors in the control of cell growth, differentiation, and development. By using transient transfection analysis of COS cells, we show that in the absence of its E protein target, the Id3 protein is localized exclusively to the cytoplasm/perinuclear region. Co-transfection with E protein (E47) results in nuclear translocation of the Id3 protein, a process requiring both a functional Id helix-loop-helix dimerization domain and an E protein nuclear localization signal. Id3 that is associated with E protein displays an extended half-life, while the E protein itself is more rapidly turned over. These observations demonstrate that E protein, by nuclear chaperoning Id, can regulate the available cellular pool of its own inhibitory partner.en
dc.language.isoenen
dc.subjectCancer Proteinsen
dc.subject.meshAnimals-
dc.subject.meshCOS Cells-
dc.subject.meshCell Compartmentation-
dc.subject.meshCell Nucleus-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshHelix-Loop-Helix Motifs-
dc.subject.meshHumans-
dc.subject.meshInhibitor of Differentiation Proteins-
dc.subject.meshMolecular Chaperones-
dc.subject.meshNeoplasm Proteins-
dc.subject.meshPrecipitin Tests-
dc.subject.meshProtein Binding-
dc.subject.meshRecombinant Proteins-
dc.subject.meshStructure-Activity Relationship-
dc.subject.meshTCF Transcription Factors-
dc.subject.meshTranscription Factors-
dc.subject.meshTransfection-
dc.titleNuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.en
dc.typeArticleen
dc.contributor.departmentCancer Research Campaign Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital National Health Service Trust, Wilmslow Road, Manchester M20 9BX, United Kingdom.en
dc.identifier.journalThe Journal of Biological Chemistryen

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