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Molecular Pharmacology

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Research ArticleMinireview—A Latin American Perspective On G Protein-Coupled Receptors

The Follitropin Receptor: Matching Structure and Function

Alfredo Ulloa-Aguirre and Teresa Zariñán
Molecular Pharmacology November 2016, 90 (5) 596-608; DOI: https://doi.org/10.1124/mol.116.104398
Alfredo Ulloa-Aguirre
Research Support Network, National University of Mexico and National Institutes of Health, Mexico City, Mexico
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Teresa Zariñán
Research Support Network, National University of Mexico and National Institutes of Health, Mexico City, Mexico
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This article has a correction. Please see:

  • Corrections to “The Follitropin Receptor: Matching Structure and Function” - January 01, 2017

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Abstract

Follitropin, or follicle-stimulating hormone (FSH) receptor (FSHR), is a G protein-coupled receptor belonging to the glycoprotein hormone receptor family that plays an essential role in reproduction. Although its primary location is the gonad, the FSHR has also been reported in extragonadal tissues including bone, placenta, endometrium, liver, and blood vessels from a number of malignant tumors. The recently resolved crystal structure of FSH bound to the entire FSHR ectodomain has been instrumental in more clearly defining the role of this domain in ligand binding and receptor activation. Biochemical, biophysical, and structural data also indicate that the FSHR exists as a higher order structure and that it may heterodimerize with its closely related receptor, the luteinizing hormone receptor; this association may have physiologic implications during ovarian follicle maturation given that both receptors may simultaneously coexist in the same cell. FSHR heterodimerization is unique to the ovary because in the testes, gonadotropin receptors are expressed in separate compartments. FSHR self-association appears to be required for receptor coupling to multiple effectors and adaptors, for the activation of multiple signaling pathways and the transduction of asymmetric signaling, and for negative and positive receptor cooperativity. It also provides a mechanism through which the glycosylation variants of FSH may exert distinct and differential effects at the target cell level. Given its importance in regulating activation of distinct signaling pathways, functional selectivity at the FSHR is briefly discussed, as well as the potential implications of this particular functional feature on the design of new pharmacological therapies in reproduction.

Footnotes

    • Received March 21, 2016.
    • Accepted June 28, 2016.
  • Research in the authors' laboratory is supported by the Consejo Nacional de Ciencia y Tecnología (CONACyT), Mexico [grant 240619], and the Coordinación de la Investigación Científica, Universidad Nacional autónoma de México (UNAM).

  • dx.doi.org/10.1124/mol.116.104398.

  • Copyright © 2016 by The American Society for Pharmacology and Experimental Therapeutics
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Molecular Pharmacology: 90 (5)
Molecular Pharmacology
Vol. 90, Issue 5
1 Nov 2016
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Research ArticleMinireview—A Latin American Perspective On G Protein-Coupled Receptors

Follitropin Receptor Structure and Function

Alfredo Ulloa-Aguirre and Teresa Zariñán
Molecular Pharmacology November 1, 2016, 90 (5) 596-608; DOI: https://doi.org/10.1124/mol.116.104398

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Research ArticleMinireview—A Latin American Perspective On G Protein-Coupled Receptors

Follitropin Receptor Structure and Function

Alfredo Ulloa-Aguirre and Teresa Zariñán
Molecular Pharmacology November 1, 2016, 90 (5) 596-608; DOI: https://doi.org/10.1124/mol.116.104398
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  • Article
    • Visual Overview
    • Abstract
    • Introduction
    • FSHR Structure
    • Extragonadal Expression of the FSHR
    • Ligand Binding and Receptor Activation: Role of the FSHR Ectodomain
    • FSHR Self-Association
    • Signal Transduction at the FSHR: Multiple Interacting Partners, Signaling Networks, and Functional Selectivity
    • Concluding Remarks
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