Nuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism.
AffiliationCancer Research Campaign Department of Gene Regulation, Paterson Institute for Cancer Research, Christie Hospital National Health Service Trust, Wilmslow Road, Manchester M20 9BX, United Kingdom.
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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.
CitationNuclear localization and regulation of Id protein through an E protein-mediated chaperone mechanism. 1996, 271 (39):23603-6 J. Biol. Chem.
JournalThe Journal of Biological Chemistry