Microfibrillar proteins MAGP-1 and MAGP-2 induce Notch1 extracellular domain dissociation and receptor activation (Q28298567)

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Rhiana Lau

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Patrick W Hein

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J Michael Shipley

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Gerry Weinmaster

Journal of Biological Chemistry

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language of work or name

English

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publication date

14 April 2006

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published in

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volume

281

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page(s)

10089-97

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issue

15

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cites work

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Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia

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Notch subunit heterodimerization and prevention of ligand-independent proteolytic activation depend, respectively, on a novel domain and the LNR repeats

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The extracellular matrix protein MAGP-2 interacts with Jagged1 and induces its shedding from the cell surface

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Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils

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Further characterization of proteins associated with elastic fiber microfibrils including the molecular cloning of MAGP-2 (MP25)

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Identification of a matrix-binding domain in MAGP1 and MAGP2 and intracellular localization of alternative splice forms

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MAGP-2 has multiple binding regions on fibrillins and has covalent periodic association with fibrillin-containing microfibrils

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Microfibril-associated glycoprotein-2 interacts with fibrillin-1 and fibrillin-2 suggesting a role for MAGP-2 in elastic fiber assembly

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The microfibrillar proteins MAGP-1 and fibrillin-1 form a ternary complex with the chondroitin sulfate proteoglycan decorin

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Microfibril-associated glycoprotein-2 specifically interacts with a range of bovine and human cell types via alphaVbeta3 integrin

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Microfibril-associated glycoprotein-2 (MAGP-2) is specifically associated with fibrillin-containing microfibrils but exhibits more restricted patterns of tissue localization and developmental expression than its structural relative MAGP-1.

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The divergent DSL ligand Dll3 does not activate Notch signaling but cell autonomously attenuates signaling induced by other DSL ligands

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Notch signaling enhances survival and alters differentiation of 32D myeloblasts

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Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment

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Antineurogenic phenotypes induced by truncated Notch proteins indicate a role in signal transduction and may point to a novel function for Notch in nuclei

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Domain-specific mutations of a transforming growth factor (TGF)-beta 1 latency-associated peptide cause Camurati-Engelmann disease because of the formation of a constitutively active form of TGF-beta 1.

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DNER acts as a neuron-specific Notch ligand during Bergmann glial development

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F3/contactin acts as a functional ligand for Notch during oligodendrocyte maturation

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NB-3/Notch1 pathway via Deltex1 promotes neural progenitor cell differentiation into oligodendrocytes.

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The nephroblastoma overexpressed gene (NOV/ccn3) protein associates with Notch1 extracellular domain and inhibits myoblast differentiation via Notch signaling pathway

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Notch signaling in vascular morphogenesis

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Mutations in the gene encoding the latency-associated peptide of TGF-β1 cause Camurati-Engelmann disease

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