(Q45318132)

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TGF-beta receptor signaling activates SMADs

An instance of the biological pathway in Homo sapiens with Reactome ID (R-HSA-2173789)

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8 July 2022

transforming growth factor beta receptor signaling pathway

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Signaling by TGF-beta Receptor Complex

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https://identifiers.org/reactome:R-HSA-2173789

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Downregulation of TGF-beta receptor signaling

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Phosphorylated SMAD2 and SMAD3 form a complex with SMAD4

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Latent TGF-beta-1 is cleaved by FURIN

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Secretion and activation of the latent large complex of TGF-beta-1

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Dimeric TGF-beta-1 binds to the receptor

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TGFBR2 recruits TGFBR1

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TGFBR2 phosphorylates TGFBR1

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An anchoring protein, ZFYVE9 (SARA), recruits SMAD2/3

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Activated type I receptor phosphorylates SMAD2/3 directly

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Phosphorylated SMAD2/3 dissociates from TGFBR

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CBL neddylates TGFBR2

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LTBP4 binds TGF-Beta-1

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Fibrillin-1 binds latent TGF-beta

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LTBP1, LTBP3 bind TGF-Beta

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Latent TGF-beta-3 binds integrins

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Latent TGF-beta-1 binds integrins

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TGF-β signalling is mediated by two autonomously functioning TβRI:TβRII pairs

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Structural basis of heteromeric smad protein assembly in TGF-beta signaling

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Ternary Complex of Transforming Growth Factor- 1 Reveals Isoform-specific Ligand Recognition and Receptor Recruitment in the Superfamily

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Mechanism of TGFbeta receptor inhibition by FKBP12

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Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors

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TGF beta signals through a heteromeric protein kinase receptor complex

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Structural basis of Smad1 activation by receptor kinase phosphorylation

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Phosphorylation of Smad signaling proteins by receptor serine/threonine kinases

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

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Cooperative assembly of TGF-beta superfamily signaling complexes is mediated by two disparate mechanisms and distinct modes of receptor binding

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Making sense of latent TGFbeta activation

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Mechanism of activation of the TGF-beta receptor

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Processing of transforming growth factor beta 1 precursor by human furin convertase

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Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses

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

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The transforming growth factor beta receptors types I, II, and III form hetero-oligomeric complexes in the presence of ligand

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TGF-beta activation by traction?

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TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4

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Cloning of a TGF beta type I receptor that forms a heteromeric complex with the TGF beta type II receptor

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Identifiers

1 reference

8 July 2022

(Q45318132)

TGF-beta receptor signaling activates SMADs

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