A Tale of Two Proteins: Betaglycan, IGSF1, and the Continuing Search for the Inhibin B Receptor.


Journal

Trends in endocrinology and metabolism: TEM
ISSN: 1879-3061
Titre abrégé: Trends Endocrinol Metab
Pays: United States
ID NLM: 9001516

Informations de publication

Date de publication:
01 2020
Historique:
received: 26 06 2019
revised: 28 08 2019
accepted: 29 08 2019
pubmed: 28 10 2019
medline: 29 7 2021
entrez: 26 10 2019
Statut: ppublish

Résumé

Inhibins are gonadal hormones that suppress follicle-stimulating hormone (FSH) synthesis by pituitary gonadotrope cells. The structurally related activins stimulate FSH by signaling through complexes of type I and type II receptors. Two models of inhibin action were proposed in 2000. First, inhibins function as competitive receptor antagonists, binding activin type II receptors with high affinity in the presence of the TGF-β type III coreceptor, betaglycan. Second, immunoglobulin superfamily, member 1 (IGSF1, then called p120) was proposed to mediate inhibin B antagonism of activin signaling via its type I receptor. These ideas have been challenged over the past few years. Rather than playing a role in inhibin action, IGSF1 is involved in the central control of the thyroid gland. Betaglycan binds inhibin A and inhibin B with high affinity, but only functions as an obligate inhibin A coreceptor in murine gonadotropes. There is likely to be a distinct, but currently unidentified coreceptor for inhibin B.

Identifiants

pubmed: 31648935
pii: S1043-2760(19)30181-X
doi: 10.1016/j.tem.2019.08.014
pii:
doi:

Substances chimiques

IGSF1 protein, human 0
Immunoglobulins 0
Membrane Proteins 0
Proteoglycans 0
Receptors, Transforming Growth Factor beta 0
betaglycan 145170-29-2
Inhibins 57285-09-3

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

37-45

Informations de copyright

Copyright © 2019 Elsevier Ltd. All rights reserved.

Auteurs

Daniel J Bernard (DJ)

Department of Pharmacology and Therapeutics, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada, H3G 1Y6; Department of Anatomy and Cell Biology, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada, H3G 1Y6. Electronic address: daniel.bernard@mcgill.ca.

Courtney L Smith (CL)

Department of Pharmacology and Therapeutics, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada, H3G 1Y6.

Emilie Brûlé (E)

Department of Anatomy and Cell Biology, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada, H3G 1Y6.

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Classifications MeSH