Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2

Notch receptors are normally cleaved during maturation by a furin-like protease at an extracellular site termed S1, creating a heterodimer of non-covalently associated subunits. The S1 site lies within a key negative regulatory region (NRR) of the receptor, which contains three highly conserved Lin1...

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Veröffentlicht in:	PLoS One 2009-08, Vol.4 (8), p.e6613-e6613
Hauptverfasser:	Gordon, Wendy R, Vardar-Ulu, Didem, L'Heureux, Sarah, Ashworth, Todd, Malecki, Michael J, Sanchez-Irizarry, Cheryll, McArthur, Debbie G, Histen, Gavin, Mitchell, Jennifer L, Aster, Jon C, Blacklow, Stephen C
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation Acute lymphoblastic leukemia Amino Acid Sequence Amino acids Analysis Antibiotics BASIC BIOLOGICAL SCIENCES Binding sites Biochemistry Biophysics/Cell Signaling and Trafficking Structures Biophysics/Structural Genomics Cell Biology/Cell Signaling Cell surface CLEAVAGE CONFORMATIONAL CHANGES Developmental Biology/Developmental Molecular Mechanisms Dimerization Drosophila Epidermal growth factor Exports Furin Furin - metabolism GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE Humans Hydrolysis Insects International trade LEUKEMIA Ligands Low density lipoprotein receptors Lymphocytes T Medical schools Metalloproteinase Models, Molecular Molecular Sequence Data Mutation MUTATIONS NMR Notch protein Notch1 protein Notch2 protein Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Pathology Proteases Protein Conformation PROTEINS Receptor mechanisms Receptor, Notch1 - chemistry Receptor, Notch1 - genetics Receptor, Notch1 - metabolism Receptor, Notch2 - chemistry Receptor, Notch2 - genetics Receptor, Notch2 - metabolism Receptors Regulation Sequence Homology, Amino Acid Signal Transduction Signaling Womens health X-Ray Diffraction
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