Inhibin binding protein (InhBP/p120), betaglycan, and the continuing search for the inhibin receptor.
Betaglycan (the TGFbeta type III receptor) and InhBP/p120 (a membrane-tethered proteoglycan) were recently identified as putative inhibin receptors. Here, we review the current state of knowledge regarding these two proteins with respect to their potential roles in inhibin biology. Importantly, neither protein appears to satisfy all of the criteria required for classification as a bona fide inhibin receptor. Betaglycan does not appear to be expressed in pituitary gonadotropes, the primary target of circulating inhibins, and InhBP/p120 does not bind inhibins in conventional receptor binding assays. While both proteins appear capable of promoting inhibin-mediated antagonism of activin signaling, neither appears to generate inhibin-specific intracellular signals. Recently, additional inhibin binding proteins were identified in inhibin target tissues, including pituitary and Leydig cells. Characterization of these proteins, coupled with ongoing investigations of betaglycan and InhBP/p120, will lead to a clearer understanding of mechanisms of inhibin action.
Bernard
Daniel J
DJ
Department of Neurobiology and Physiology, Northwestern University, Evanston, Illinois 60208, USA.
Chapman
Stacey C
SC
Woodruff
Teresa K
TK
D029404:Activin Receptors; D028341:Activins / Q000378:metabolism; D000818:Animals; D005260:Female; D006801:Humans; D007985:Leydig Cells / Q000378:metabolism; D008297:Male; D010053:Ovary / Q000378:metabolism; D010902:Pituitary Gland / Q000166:cytology / Q000378:metabolism; D011509:Proteoglycans / Q000378:metabolism*; D018000:Receptors, Peptide / Q000378:metabolism*; D018125:Receptors, Transforming Growth Factor beta / Q000378:metabolism*; D015398:Signal Transduction; D013379:Substrate Specificity
D011509:Proteoglycans; D018000:Receptors, Peptide; D018125:Receptors, Transforming Growth Factor beta; D028341:Activins; C071736:betaglycan; D029404:Activin Receptors