A Ligand-Induced Extracellular Cleavage Regulates γ-Secretase-like Proteolytic Activation of Notch1

γ-secretase-like proteolysis at site 3 (S3), within the transmembrane domain, releases the N otch i ntra c ellular d omain (NICD) and activates CSL-mediated Notch signaling. S3 processing occurs only in response to ligand binding; however, the molecular basis of this regulation is unknown. Here we d...

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Veröffentlicht in:	Molecular cell 2000-02, Vol.5 (2), p.197-206
Hauptverfasser:	Mumm, Jeffrey S, Schroeter, Eric H, Saxena, Meera T, Griesemer, Adam, Tian, Xiaolin, Pan, D.J, Ray, William J, Kopan, Raphael
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amyloid Precursor Protein Secretases Conserved Sequence Cysteine - genetics Disintegrins - metabolism Drosophila Proteins Endopeptidases - metabolism g-secretase Ligands Membrane Proteins - genetics Membrane Proteins - metabolism Metalloendopeptidases - metabolism Mutation NEXT protein NICD protein Notch1 protein Peptide Fragments - genetics Peptide Fragments - metabolism Presenilin-1 Protein Processing, Post-Translational Receptor, Notch1 Receptors, Cell Surface - genetics Receptors, Cell Surface - metabolism Signal Transduction Transcription Factors
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