Naturally Occurring Mutants Inform SHBG Structure and Function
Open accessAbstract
SHBG transports and regulates the activities of androgens and estrogens. Several single nucleotide polymorphisms in the human SHBG gene have been linked to sex steroid-dependent diseases, including those associated with the metabolic syndrome. The N-terminal laminin G-like domain of SHBG includes binding sites for calcium, sex steroids, and fibulin family members, as well as a dimerization domain. We have found that 8 of 18 uncharacterized nonsynonymous single nucleotide polymorphisms within this domain alter the production or biochemical properties of SHBG in ways not previously recognized. O-Linked glycosylation at Thr7 is disrupted in SHBG T7N, whereas abnormal glycosylation of SHBG G195E limits its secretion. Three SHBG mutants (R135C, L165M, and E176K) bind estradiol with abnormally high affinity. SHBG R135C also has an increased interaction with fibulin-2. Two different substitutions within the dimer interface at R123 (R123H and R123C) reduce the affinity for 5α-dihydrotestosterone, while increasing the relative binding affinity for estradiol. SHBG T48I is defective in calcium binding, which leads to a defect in dimerization, reduced affinity for sex steroids, and an enhanced interaction with fibulin-2, which can all be restored by calcium supplementation. These naturally occurring mutants provide insight into SHBG structure and function, and defects in SHBG production or function need to be considered in the context of its utility as a biomarker of diseases.
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Genetic variation in SHBG alters the binding affinity constant for testosterone and DHT.
“However, genetic variation in SHBG also alters the binding affinity constant for T and DHT [42].”
From Role of sex hormone-binding globulin in the free hormone hypothesis and the relevance of free testosterone in androgen physiology (2022) · cites this paper as [42]
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- Authors
- Wu, T.-S., & Hammond, G. L.
- Affiliations
- University of British Columbia (CA)
- Corresponding author
- Hammond, Geoffrey L.
- ORCID
- Hammond, Geoffrey L.
- Venue
- Molecular Endocrinology
- Publisher
- The Endocrine Society
- Published
- 2014-07-01
- Volume
- 28
- Issue
- 7
- Pages
- 1026-1038
- ISSN
- 0888-8809 (ISSN-L)
- 1944-9917
- PMC
- PMC5414826
- OpenAlex
- W2098796594
- Cited by
- 40
- References
- 42
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 6 · 2023: 3 · 2022: 3 · 2021: 4 · 2020: 4 · 2019: 3 · 2018: 1 · 2017: 4 · 2016: 5 · 2015: 1 · 2014: 2
- FWCI
- 2.63
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Endocrinology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- University of British Columbia
- National Institutes of Health
- Canadian Institutes of Health Research (MOP 15261)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Estrogen and related hormone effects
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Hormonal and reproductive studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
- Keywords
- sex hormone-binding globulin, single nucleotide polymorphisms, estradiol binding, dihydrotestosterone, fibulin-2, calcium binding, dimerization, O-glycosylation, protein secretion, metabolic syndrome, biomarkers
- MeSH terms
- Animals, Binding Sites, Calcium, Calcium-Binding Proteins, Cell Line, Cricetulus, Estradiol, Glycosylation, Humans, Protein Binding, Receptors, Cell Surface, Recombinant Proteins, Sex Hormone-Binding Globulin, Dihydrotestosterone, Extracellular Matrix Proteins, Sequence Alignment, CHO Cells, Protein Structure, Tertiary, Polymorphism, Single Nucleotide, Protein Multimerization
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