Identification of human activin and TGFβ type I receptors that form heteromeric kinase complexes with type II receptors

@article{Attisano1993IdentificationOH,
  title={Identification of human activin and TGF$\beta$ type I receptors that form heteromeric kinase complexes with type II receptors},
  author={Liliana Attisano and Juan M. Cárcamo and Francesc Ventura and F M Weis and Joan Massagu{\'e} and Jeffrey L. Wrana},
  journal={Cell},
  year={1993},
  volume={75},
  pages={671-680}
}

Characterization of type I receptors for transforming growth factor-beta and activin.

A systematic analysis revealed that most ALKs formed heteromeric complexes with the type II receptors for TGF-beta and activin after overexpression in COS cells; however, among the six ALK’s, only ALK-5 was a functional T GF-beta type I receptor for activation of plasminogen activator inhibitor-1, and only ALF-4 bound activin with high affinity.

Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin

It is concluded that the type I receptor subunits are primary specifiers of signals sent by TGF-beta and activin receptor complexes and do not substitute as mediators of these growth-inhibitory and extracellular matrix transcriptional responses.

Inactivation of activin-dependent transcription by kinase-deficient activin receptors.

It is indicated that kinase activities of both type II and type I receptors are required for activin signaling, and that the two types I receptors, which are expressed in a tissue-specific manner, are functionally distinct.

Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation

It is demonstrated here that activin specifically induces heteromer formation between the type I and type II receptors in a time-dependent manner, which results in an increase in the hemoglobin content of the cells and limits their proliferation.

Formation and activation by phosphorylation of activin receptor complexes.

Analysis of the interaction between various activin receptors revealed that ActRs I and II could exist in a stable complex and that formation of that complex between transiently overexpressed molecules was not regulated by ligand, supporting a role for phosphorylation of type I ActRs in the generation of a biological signal.

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

The specific interaction between the type I receptors and FKBP-12 suggests that FK BP-12 may play a role in type I receptor-mediated signaling.

Ligand-independent Activation of Transforming Growth Factor (TGF) β Signaling Pathways by Heteromeric Cytoplasmic Domains of TGF-β Receptors*

The results indicate that the cytoplasmic domains of the type I and type II TGF-β receptors physically and functionally interact with each other in the heteromeric complex.

Two distinct transmembrane serine/threonine kinases from Drosophila melanogaster form an activin receptor complex

The results indicate that the heteromeric kinase structure is a general feature of this receptor family and defines Atr-I as an activin type I receptor from D. melanogaster.

Signal transduction and TGF-beta superfamily receptors.

Although a number of transduction mechanisms may be available to TGF-beta superfamily members, evidence gathered through the use of specific kinase and G-protein inhibitors and through assays measuring activation and levels of signaling intermediates suggests that at least one signaling pathway interacts with Ras and Raf proteins via a G- protein intermediate.
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References

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Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor.

Combinatorial interactions and stoichiometric ratios between the type I and II receptors may determine the extent of TGF-beta binding and the resulting biological activities.

Identification of a Drosophila activin receptor.

The identification, deduced primary structure, and expression pattern of Atr-II, a receptor serine/threonine kinase found in Drosophila, is described and the possible role of an activin signaling system in Dosophila development is discussed.

A surface component on GH3 pituitary cells that recognizes transforming growth factor-beta, activin, and inhibin.

The 70-74-kDa labeled GH3 components represent a novel type of cell surface TGF-beta binding protein that is unique in its ability to recognize various other members of the T GF-beta family of bioactive polypeptides.
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