Probing the role of homomeric and heteromeric receptor interactions in TGF-β signaling using small molecule dimerizers

@article{Stockwell1998ProbingTR,
  title={Probing the role of homomeric and heteromeric receptor interactions in TGF-β signaling using small molecule dimerizers},
  author={B. Stockwell and S. Schreiber},
  journal={Current Biology},
  year={1998},
  volume={8},
  pages={761-773}
}
  • B. Stockwell, S. Schreiber
  • Published 1998
  • Biology, Medicine
  • Current Biology
    • BACKGROUND Transforming growth factor Beta (TGF-Beta) arrests many cell types in the G1 phase of the cell and upregulates plasminogen activator inhibitor 1 (PAI-1). The type 1 (TGF-Beta RI) an II (TGF-Beta RII) TGF-Beta receptors mediate these and other effects of TGF-Beta on target cells. TGF-Beta initially binds to TGF-Beta RII and subsequently TGF-Beta RI is recruited to form a heteromeric complex. TGF-Beta RI phosphorylates the downstream effectors Smad2 and Smad3, leading to their… CONTINUE READING
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    References

    SHOWING 1-10 OF 86 REFERENCES
    Ligand-induced dimerization of the extracellular domain of the TGF-beta receptor type II.
    • 13
    A single heteromeric receptor complex is sufficient to mediate biological effects of transforming growth factor-beta ligands.
    • 49
    • PDF
    Homomeric interactions between type II transforming growth factor-beta receptors.
    • 131
    TGF-β-signaling with small molecule FKBP12 antagonists that bind myristoylated FKBP12-TGF-β type I receptor fusion proteins
    • 30
    The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands.
    • 114
    Biochemical evidence for the autophosphorylation and transphosphorylation of transforming growth factor beta receptor kinases.
    • F. Chen, R. Weinberg
    • Biology, Medicine
    • Proceedings of the National Academy of Sciences of the United States of America
    • 1995
    • 121
    • Highly Influential
    • PDF
    The Soluble Exoplasmic Domain of the Type II Transforming Growth Factor (TGF)-β Receptor
    • 13
    • PDF
    Signaling Activity of Homologous and Heterologous Transforming Growth Factor-β Receptor Kinase Complexes (*)
    • 83
    • PDF
    Ligand-independent Activation of Transforming Growth Factor (TGF) β Signaling Pathways by Heteromeric Cytoplasmic Domains of TGF-β Receptors*
    • 112
    • PDF
    Disruption of transforming growth factor beta signaling by a mutation that prevents transphosphorylation within the receptor complex.
    • 226
    • PDF