Science · 2001 · 41 citations · 4 references
Life SciencesCell BiologyMolecular BiologyCell SignalingGene ExpressionSignal TransductionLigand BindingProtein Kinase CascadesReceptor Tyrosine Kinase SignalingReceptor-mediated SignalingSignal Transduction PathwaysTranscriptional Regulation In EukaryotesErbb Receptor SignalingLigand-induced Receptor ActivationReceptor Proteolytic CleavageReceptor Tyrosine Kinase CascadesRegulated Intramembrane ProteolysisTransmembrane ProteinsTyrosine Kinase Receptor SignalingTyrosine Kinase Receptors
A ligand binding to its transmembrane receptor can activate several different signaling pathways that indirectly switch on the transcription of target genes in the nucleus. As [Heldin and Ericsson][1] explain in their Perspective, new findings reveal that some receptors such as ErbB-4 can also take a more direct approach to activating gene transcription ([ Ni et al .][2]). Once bound to ligand, ErbB-4 is proteolytically cleaved twice. First the ectodomain is released, then intramembrane cleavage releases a cytoplasmic fragment, which moves to the nucleus where it may affect gene expression. [1]: http://www.sciencemag.org/cgi/content/full/294/5549/2111 [2]: http://www.sciencemag.org/cgi/content/short/294/5549/2179
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γ-Secretase Cleavage and Nuclear Localization of ErbB-4 Receptor Tyrosine Kinase
Chang-Yuan Ni, M. Paul Murphy, Todd E. Golde et al. · Science · 2001 · 858 citations
W. Taylor Kimberly, Jessica B. Zheng, Suzanne Y. Guénette et al. · Journal of Biological Chemistry · 2001 · 437 citations · Full text
p300 Acts as a Transcriptional Coactivator for Mammalian Notch-1
Franz Oswald, Birgitt Täuber, Thomas Dobner et al. · Molecular and Cellular Biology · 2001 · 327 citations · Full text