Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Positive and negative regulation of type II TGF-beta receptor signal transduction by autophosphorylation on multiple serine residues.

The EMBO journal - 15 Apr 1997

Luo K, Lodish H F

Abstract excerpt

The type II transforming growth factor-beta (TGF-beta) receptor Ser/Thr kinase (TbetaRII) is responsible for the initiation of multiple TGF-beta signaling pathways, and loss of its function is associated with many types of human cancer. Here we show that TbetaRII kinase is regulated intricately by autophosphorylation on at least three serine residues. Ser213, in the membrane-proximal segment outside the kinase...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to B-Lymphocytes
Share to Cell Line

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Phosphorylation

Share to Protein Serine-Threonine Kinases

Share to Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 9155023
DOI: 10.1093/emboj/16.8.1970
PMCID: PMC1169800

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Positive and negative regulation of type II TGF-beta receptor signal transduction by autophosphorylation on multiple serine residues.PMID 9155023Read ↗

Three key residues underlie the differential affinity of the TGFbeta isoforms for the TGFbeta type II receptor.Semantic proximity Read ↗

Complementation between kinase-defective and activation-defective TGF-beta receptors reveals a novel form of receptor cooperativity essential for signaling.Semantic proximity Read ↗

Phosphorylation of Ser165 in TGF-beta type I receptor modulates TGF-beta1-induced cellular responses.Semantic proximity Read ↗

The balance of cell surface and soluble type III TGF-β receptor regulates BMP signaling in normal and cancerous mammary epithelial cells.Semantic proximity Read ↗

Smad2 phosphorylation by type I receptor: contribution of arginine 462 and cysteine 463 In the C terminus of Smad2 for specificity.Semantic proximity Read ↗

Modulation of the functional binding sites for TGF-beta on the type II receptor leads to suppression of TGF-beta signaling.Semantic proximity Read ↗

In silico analysis of the potential effects of the disease-associated point mutations on the kinase activity of TGFBR1 and TGFBR2 receptorsSemantic proximity Read ↗

Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies.Semantic proximity Read ↗

Constitutive homo- and hetero-oligomerization of TbetaRII-B, an alternatively spliced variant of the mouse TGF-beta type II receptor.Semantic proximity Read ↗

Structural basis for specificity of TGFβ family receptor small molecule inhibitors.Semantic proximity Read ↗

Ectodomain shedding of TβRIII is required for TβRIII-mediated suppression of TGF-β signaling and breast cancer migration and invasion.Semantic proximity Read ↗

Autoinhibitory mechanisms in receptor tyrosine kinases.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.