(Q27635175)

1

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T W Muir

2

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L Xu

3

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Y G Chen

4

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J Kuriyan

5

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J Massagué

TbetaRI phosphorylation of Smad2 on Ser465 and Ser467 is required for Smad2-Smad4 complex formation and signaling

6

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publication date

September 2001

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published in

Molecular Cell

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volume

8

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page(s)

671-82

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issue

3

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cites work

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Purification and characterization of recombinant human p50csk protein-tyrosine kinase from an Escherichia coli expression system overproducing the bacterial chaperones GroES and GroEL.

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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Smad4 and FAST-1 in the assembly of activin-responsive factor

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Mechanism of TGFbeta receptor inhibition by FKBP12

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Determinants of specificity in TGF-beta signal transduction.

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Synthesis of proteins by native chemical ligation

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The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms

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A kinase subdomain of transforming growth factor-beta (TGF-beta) type I receptor determines the TGF-beta intracellular signaling specificity

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Mutations increasing autoinhibition inactivate tumour suppressors Smad2 and Smad4.

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Crystal structure of the cytoplasmic domain of the type I TGF beta receptor in complex with FKBP12

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Active and inactive protein kinases: structural basis for regulation

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Drosophila Mad binds to DNA and directly mediates activation of vestigial by Decapentaplegic

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Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53

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Dual role of the Smad4/DPC4 tumor suppressor in TGFbeta-inducible transcriptional complexes

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

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TGF-beta signal transduction

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Phosphorylation of Ser465 and Ser467 in the C terminus of Smad2 mediates interaction with Smad4 and is required for transforming growth factor-beta signaling

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SARA, a FYVE domain protein that recruits Smad2 to the TGFbeta receptor

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

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Structural basis of Smad2 recognition by the Smad anchor for receptor activation

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Grabbing phosphoproteins

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

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