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Science 1 January 1999:
Vol. 283. no. 5398, pp. 91 - 94
DOI: 10.1126/science.283.5398.91
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Reports

Processing of the Notch Ligand Delta by the Metalloprotease Kuzbanian

Huilin Qi, *dagger Matthew D. Rand, *dagger Xiaohui Wu, Nenad Sestan, Weiyi Wang, Pasko Rakic, Tian Xu, Spyros Artavanis-Tsakonas dagger ddagger

Signaling by the Notch surface receptor controls cell fate determination in a broad spectrum of tissues. This signaling is triggered by the interaction of the Notch protein with what, so far, have been thought to be transmembrane ligands expressed on adjacent cells. Here biochemical and genetic analyses show that the ligand Delta is cleaved on the surface, releasing an extracellular fragment capable of binding to Notch and acting as an agonist of Notch activity. The ADAM disintegrin metalloprotease Kuzbanian is required for this processing event. These observations raise the possibility that Notch signaling in vivo is modulated by soluble forms of the Notch ligands.

H. Qi, M. Rand, S. Artavanis-Tsakonas, Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536-0812, USA. X. Wu, Department of Genetics, Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536-0812, USA, and Institute of Genetics, Fudan University, 220 Handan Road, Shanghai 200433, People's Republic of China. N. Sestan and P. Rakic, Section of Neurobiology, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536-0812, USA. W. Wang and T. Xu, Department of Genetics, Howard Hughes Medical Institute, Yale University School of Medicine, Boyer Center for Molecular Medicine, 295 Congress Avenue, New Haven, CT 06536-0812, USA.
*   These authors contributed equally to this work.

dagger    Present address: Harvard Medical School, Massachussetts General Hospital Cancer Center, Building 149, 13th Street, Charlestown, MA 02129, USA.

ddagger    To whom correspondence should be addressed.

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Antagonism of notch signaling activity by members of a novel protein family encoded by the bearded and enhancer of split gene complexes.
E. Lai, R Bodner, J Kavaler, G Freschi, and J. Posakony (2000)
Development 127, 291-306
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Interaction of the Metalloprotease Disintegrins MDC9 and MDC15 with Two SH3 Domain-containing Proteins, Endophilin I and SH3PX1.
L. Howard, K. K. Nelson, R. A. Maciewicz, and C. P. Blobel (1999)
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Specific Sequence Elements Are Required for the Expression of Functional Tumor Necrosis Factor-alpha -converting Enzyme (TACE).
M. E. Milla, M. A. Leesnitzer, M. L. Moss, W. C. Clay, H. L. Carter, A. B. Miller, J.-L. Su, M. H. Lambert, D. H. Willard, D. M. Sheeley, et al. (1999)
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Contact-Dependent Inhibition of Cortical Neurite Growth Mediated by Notch Signaling.
N. Sestan, S. Artavanis-Tsakonas, and P. Rakic (1999)
Science 286, 741-746
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MDC-L, a Novel Metalloprotease Disintegrin Cysteine-rich Protein Family Member Expressed by Human Lymphocytes.
C. M. Roberts, P. H. Tani, L. C. Bridges, Z. Laszik, and R. D. Bowditch (1999)
J. Biol. Chem. 274, 29251-29259
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Cloning and Characterization of ADAMTS11, an Aggrecanase from the ADAMTS Family.
I. Abbaszade, R.-Q. Liu, F. Yang, S. A. Rosenfeld, O. H. Ross, J. R. Link, D. M. Ellis, M. D. Tortorella, M. A. Pratta, J. M. Hollis, et al. (1999)
J. Biol. Chem. 274, 23443-23450
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Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor.
J. Dong, L. K. Opresko, P. J. Dempsey, D. A. Lauffenburger, R. J. Coffey, and H. S. Wiley (1999)
PNAS 96, 6235-6240
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Notch Signaling: Cell Fate Control and Signal Integration in Development.
S. Artavanis-Tsakonas, M. D. Rand, and R. J. Lake (1999)
Science 284, 770-776
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Constitutive and regulated alpha -secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease.
S. Lammich, E. Kojro, R. Postina, S. Gilbert, R. Pfeiffer, M. Jasionowski, C. Haass, and F. Fahrenholz (1999)
PNAS 96, 3922-3927
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Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding.
J Schlondorff and C. Blobel (1999)
J. Cell Sci. 112, 3603-3617
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Notch and the CD4 Versus CD8 Lineage Decision.
P. VALDEZ and E. ROBEY (1999)
Cold Spring Harb Symp Quant Biol 64, 27-32
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RGD-independent Binding of Integrin alpha 9beta 1 to the ADAM-12 and -15 Disintegrin Domains Mediates Cell-Cell Interaction.
K. Eto, W. Puzon-McLaughlin, D. Sheppard, A. Sehara-Fujisawa, X.-P. Zhang, and Y. Takada (2000)
J. Biol. Chem. 275, 34922-34930
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Suppression of Erythroid but Not Megakaryocytic Differentiation of Human K562 Erythroleukemic Cells by Notch-1.
L. T. Lam, C. Ronchini, J. Norton, A. J. Capobianco, and E. H. Bresnick (2000)
J. Biol. Chem. 275, 19676-19684
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Dm1-MMP, a Matrix Metalloproteinase from Drosophila with a Potential Role in Extracellular Matrix Remodeling during Neural Development.
E. Llano, A. M. Pendas, P. Aza-Blanc, T. B. Kornberg, and C. Lopez-Otin (2000)
J. Biol. Chem. 275, 35978-35985
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Cleavage and Shedding of E-cadherin after Induction of Apoptosis.
U. Steinhusen, J. Weiske, V. Badock, R. Tauber, K. Bommert, and O. Huber (2001)
J. Biol. Chem. 276, 4972-4980
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