MADR2 is a substrate of the TGFbeta receptor and its phosphorylation is required for nuclear accumulation and signaling (Q24310282)

GOA release 2020-03-11

SMAD family member 2

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type I transforming growth factor beta receptor binding

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author name string

M Macías-Silva

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S Abdollah

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P A Hoodless

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R Pirone

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L Attisano

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J L Wrana

TGF-beta receptors and actions

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language of work or name

English

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publication date

27 December 1996

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1215-24

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cites work

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A novel mesoderm inducer, Madr2, functions in the activin signal transduction pathway

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Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates

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Disruption of transforming growth factor beta signaling by a mutation that prevents transphosphorylation within the receptor complex.

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A WD-domain protein that is associated with and phosphorylated by the type II TGF-beta receptor

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MADR2 maps to 18q21 and encodes a TGFbeta-regulated MAD-related protein that is functionally mutated in colorectal carcinoma

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Xenopus Mad proteins transduce distinct subsets of signals for the TGF beta superfamily

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DPC4, a candidate tumor suppressor gene at human chromosome 18q21.1

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Cloning of a novel type II serine/threonine kinase receptor through interaction with the type I transforming growth factor-beta receptor

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What do BMPs do in mammals? Clues from the mouse short-ear mutation

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Serine phosphorylation, chromosomal localization, and transforming growth factor-beta signal transduction by human bsp-1

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A human Mad protein acting as a BMP-regulated transcriptional activator

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Identification of receptors for type-beta transforming growth factor

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TGFbeta signaling: receptors, transducers, and Mad proteins.

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XTcf-3 transcription factor mediates beta-catenin-induced axis formation in Xenopus embryos

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Caenorhabditis elegans genes sma-2, sma-3, and sma-4 define a conserved family of transforming growth factor beta pathway components

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Interaction of transforming growth factor-beta receptor I with farnesyl-protein transferase-alpha in yeast and mammalian cells

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Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12

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The p21(RAS) farnesyltransferase alpha subunit in TGF-beta and activin signaling

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The immunophilin FKBP12 functions as a common inhibitor of the TGF beta family type I receptors.

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Mechanism of activation of the TGF-beta receptor

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Mammalian dwarfins are phosphorylated in response to transforming growth factor beta and are implicated in control of cell growth

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Receptor-associated Mad homologues synergize as effectors of the TGF-beta response

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