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PMID: 10611754, 9759503, 9393997, 9561843 Receptor complexes are heterotetrameric, consisting of two ‘type II' receptors (75–85 kDa), which bind ligand, and two signal transducing ‘type I' receptors (50–60 kDa) which, in most instances, cannot bind ligand directly and thus are considered to act downstream of the type II receptor. PMID: 10611754 Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).

PMID: 10611754 The assembly of the heteromeric complex is initiated by ligand binding and stabilized by interactions between the cytoplasmic domains of the type II and type I receptors. PMID: 10611754 Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).

PMID: 10611754, 10187774 Another type I receptor, ALK-1, expressed on endothelial cells and mutated in the autosomal dominant disorder hereditary hemorrhagic telangiectasia (HHT), can also complex with ligand-bound TBR-II, but its role in signaling is presently not understood.

PMID: 10611754 Signals from all three isoforms of TGF-beta appear to be mediated by a single type II receptor called TBR-II and one type I receptor referred to either as TBR-I or ALK-5 (activin receptor-like kinase).

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Betaglycan, formerly called the ‘type III receptor', binds all isoforms of TGF-beta, but may play a selective role in facilitating interaction of TGF-beta2 with TBR-II, since this isoform binds to the type II receptor with significantly lower affinity than that of TGF-beta1 and TGF-beta3.

PMID: 10611754 Unlike betaglycan, endoglin binds TGF-beta1 and TGF-beta3 selectively.

PMID: 10611754 Unlike betaglycan, endoglin binds TGF-beta1 and TGF-beta3 selectively.

PMID: 10611754 This model for receptor activation involves potentiation of the kinase activity of the type I receptor by phosphorylation of several residues in a glycine-serine-rich juxtamembrane domain (GS domain) by the type II receptor kinase.

PMID: 10611754 receptor-activated Smads bind to and are phosphorylated on two C-terminal serine residues in their MH2 domain by the type I receptor kinase.

PMID: 10611754 receptor-activated Smads bind to and are phosphorylated on two C-terminal serine residues in their MH2 domain by the type I receptor kinase.

PMID: 10611754 the phosphorylated, pathway-specific Smads then hetero-oligomerize in the cytoplasm with the common mediator, Smad4.

PMID: 10611754 the phosphorylated, pathway-specific Smads then hetero-oligomerize in the cytoplasm with the common mediator, Smad4.

PMID: 10611754 the heteromeric Smad4-containing complex is then translocated to the nucleus where it mediates transcriptional activation of the target gene.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors. PMID: 10611754 The FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir; the C-terminal domain anchors the Smad-SARA complex to the receptor complex.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors. PMID: 10611754 The FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir; the C-terminal domain anchors the Smad-SARA complex to the receptor complex.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

Indirect

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors. PMID: 10611754 Examples are the activating phosphorylation and nuclear translocation of Smad2 following treatment of cells with HGF [54] or activation of the SAPK/JNK pathway.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9311995, 8752209 Of the five receptor-activated Smads identified thus far, Smad2 and 3 have been shown to mediate signals from TGF-beta and activin receptors.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta.

PMID: 10611754, 9788633 Smad1 is phosphorylated and partners with Smad4 following treatment of human breast cancer cells with either BMP-2 or TGF-beta. PMID: 10611754 Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.

PMID: 10611754, 9214508, 9670020 Determination of the tertiary structure of the C-terminal domain of Smad4 shows that it associates as a homotrimer [25], and data now suggest that hetero-oligomeric Smads are also trimeric.

PMID: 19611754 he FYVE domain of SARA is predicted to interact with phosphosphotidyl inositol-3-phosphate in the cell membrane while an adjacent Smad binding domain recruits Smad2/3 from the cytoplasmic reservoir.

Indirect

PMID: 10611754 The mRNAs for Smad6 and Smad7 are rapidly induced by treatment of cells with TGF-beta suggesting that anti-Smads are direct effectors of a ligand-induced signal to suppress a response.

Indirect

PMID: 10611754 The mRNAs for Smad6 and Smad7 are rapidly induced by treatment of cells with TGF-beta suggesting that anti-Smads are direct effectors of a ligand-induced signal to suppress a response.

PMID: 10611754 the MH2 domain of Smad2 interacts with the C-terminal domain (Smad-interaction domain, SID) of FAST-1 directly, while the binding of Smad4 is assumed to be dependent on its association with activated Smad2 and possibly also on its ability to stabilize the DNA complex through its MH1 domain.

PMID: 10611754, 9732876 Smad3 can interact directly with c-Jun and c-Fos through its MH1 and MH2 domains, respectively leading to the suggestion that AP-1 DNA binding sites can be activated either by direct binding of Smad3 and Smad4 to the DNA element itself or by interaction of the heteromeric Smad3/Smad4 complex and the AP-1 transcription factor complex, in such a manner as to provide additional stability to the complex.

PMID: 10611754, 9732876 Smad3 can interact directly with c-Jun and c-Fos through its MH1 and MH2 domains, respectively leading to the suggestion that AP-1 DNA binding sites can be activated either by direct binding of Smad3 and Smad4 to the DNA element itself or by interaction of the heteromeric Smad3/Smad4 complex and the AP-1 transcription factor complex, in such a manner as to provide additional stability to the complex.

PMID: 10611754 These proteins have now been shown to also interact with Smad proteins in the regulation of transcription. PMID: 10611754, 9689110 The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.

PMID: 10611754, 9679060, 9865696 Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300. PMID: 10611754, 9689110 The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.

PMID: 10611754, 9679060, 9865696 Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300. PMID: 10611754, 9689110 The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.

PMID: 10611754, 9679060, 9865696 Depending on the system and the cell type, ligand-activated Smad1, Smad2, and Smad3, as well as Smad4 have all been shown to be capable of binding to CBP/p300. PMID: 10611754, 9689110 The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.

PMID: 10611754, 9689110 The essential nature of this interaction is demonstrated by the fact that disruption of the Smad-CBP/p300 interaction by the adenoviral transforming protein E1A, which binds the coactivators, blocks nearly all Smad-stimulated transcriptional responses in cells.

PMID: 10611754 Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.

PMID: 10611754 Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.

Indirect

PMID: 10611754 Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.

Indirect

PMID: 10611754 Treatment of cells with EGF or hepatocyte growth factor (HGF) results in phosphorylation of Smad1 on these sites by the Erk subfamily of MAP kinases, and in retention of the linker-region phosphorylated Smad1 in the cytoplasm, blocking the nuclear translocation and transcriptional activating activity of Smad1/Smad4 complexes.

Indirect

PMID: 10611754 Examples are the activating phosphorylation and nuclear translocation of Smad2 following treatment of cells with HGF [54] or activation of the SAPK/JNK pathway.

Indirect

PMID: 10611754, 9712726, 10067896 Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.

Indirect

PMID: 10611754, 9712726, 10067896 Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.

PMID: 10611754, 9712726, 10067896 Smad7 is also an important focal point of disparate signaling pathways as evidenced by its induction by EGF [35] and interferon.

PMID: 10611754, 9707553 Another nuclear protein that strongly activates transcription without binding to DNA, MSG1, has been shown to interact functionally with the SAD domain in the middle linker region of Smad4 and to be required for activation of Smad4-dependent transcription in certain cells.