|Receptor Transforming Growth Factor-beta Receptor, Type III||OKDB#: 916|
|Synonyms:||BETAGLYCAN|||Ovarian localization:||Primordial Germ Cell, Oocyte, Granulosa, Theca, Luteal cells, Stromal cells|
Is involved in interactions with:
TGFB2, transforming growth factor, beta 2 OKdb (Ovarian localization: )
TGFBR2, TGF-beta receptor type II precursor OKdb (Ovarian localization: Oocyte Cumulus Granulosa Theca Luteal SurfEpi)
TGFBR1, TGF-beta receptor type I precursor OKdb (Ovarian localization: Oocyte Cumulus Granulosa Theca Luteal SurfEpi)
Comments: Mechanisms of TGF-beta signaling from cell membrane to the nucleus. Cell. 2003 .
INHA, Inhibin, Alpha OKdb (Ovarian localization: Granulosa Luteal)
Comments: Inhibin is an antagonist of bone morphogenetic protein signaling.
Wiater E, Vale W.: Inhibins are endogenous antagonists of activin signaling, long recognized as important regulators of gonadal function and pituitary FSH release. Inhibin, in concert with its co-receptor, betaglycan, can compete with activin for binding to type II activin receptors and, thus, prevent activin signaling. Because bone morphogenetic proteins (BMPs) also utilize type II activin receptors, we hypothesized that BMP signaling might also be sensitive to inhibin blockade. Here we show that inhibin blocks cellular responses to diverse BMP family members in a variety of BMP-responsive cell types. Inhibin abrogates BMP-induced Smad signaling and transcription responses. Inhibin competes with BMPs for type II activin receptors, and this competition is facilitated by betaglycan. Betaglycan also enables inhibin to bind to and compete with BMPs for binding to the BMP-specific type II receptor BMPRII, which does not bind inhibin in the absence of betaglycan. Betaglycan can confer inhibin responsiveness on cells that are otherwise insensitive to inhibin. These findings demonstrate that inhibin, acting through betaglycan, can function as an antagonist of BMP responses, suggesting a broader role for inhibin and betaglycan in restricting and refining a wide spectrum of transforming growth factor beta superfamily signals.
Lewis KA, et al. (Nature. 2000) found that the type III TGF-beta receptor, betaglycan, can function as an inhibin co-receptor with ActRII. Betaglycan binds inhibin with high affinity and enhances binding in cells co-expressing ActRII and betaglycan.
Data Supplied By HPMR