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

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

Biochemical and biophysical research communications - 22 Dec 2006

Krishnaveni Manda S, Hansen Jakob Lerche, Seeger Werner, Morty Rory E, Sheikh Søren P, Eickelberg Oliver

Abstract excerpt

Transforming growth factor (TGF)-beta ligands signal through transmembrane type I and type II serine/threonine kinase receptors, which form heteromeric signalling complexes upon ligand binding. Type II TGF-beta receptors (TbetaRII) are reported to exist as homodimers at the cell surface, but the oligomerization pattern and dynamics of TbetaRII splice variants in live cells has not been demonstrated thus far....

Read the complete abstract on PubMed

Topics

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

Share to Chlorocebus aethiops
Share to Dimerization

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to NIH 3T3 Cells

Share to Organ Specificity

Share to Receptor, Transforming Growth Factor-beta Type II

Share to Receptors, Transforming Growth Factor beta

Share to RNA Splice Sites

Share to Tissue Distribution

Source

Identifiers

PMID: 17078931
DOI: 10.1016/j.bbrc.2006.10.083

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Constitutive homo- and hetero-oligomerization of TbetaRII-B, an alternatively spliced variant of the mouse TGF-beta type II receptor.PMID 17078931Read ↗

Assembly of TbetaRI:TbetaRII:TGFbeta ternary complex in vitro with receptor extracellular domains is cooperative and isoform-dependent.Semantic proximity Read ↗

In the absence of type III receptor, the transforming growth factor (TGF)-beta type II-B receptor requires the type I receptor to bind TGF-beta2.Semantic proximity Read ↗

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

TGF-beta type II receptor phosphorylates PTH receptor to integrate bone remodelling signalling.Semantic proximity Read ↗

Type I transforming growth factor beta receptor binds to and activates phosphatidylinositol 3-kinase.Semantic proximity Read ↗

A novel splice variant of human TGF-β type II receptor encodes a soluble protein and its Fc-tagged version prevents liver fibrosis <i>in vivo</i>Semantic proximity Read ↗

The mode of bone morphogenetic protein (BMP) receptor oligomerization determines different BMP-2 signaling pathways.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 ↗

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

TGF‐β signalling is mediated by two autonomously functioning TβRI:TβRII pairsSemantic proximity Read ↗

TGF-β type II receptor–deficient thymocytes develop normally but demonstrate increased CD8+ proliferation in vivoSemantic proximity Read ↗

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

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