ArticleThe Journal of biological chemistry2016
Thyroglobulin Represents a Novel Molecular Architecture of Vertebrates.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Thyroglobulin and thyroglobulin antibodies in differentiated thyroid cancer: interpretation, challenges, and future perspectives.Journal of molecular endocrinology · 2026Review
- Substrate for Thyroid Hormone Synthesis: Biochemistry, Evolution, and Physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- Thyroid Hormone Synthesis Without Thyroglobulin.Thyroid : official journal of the American Thyroid Association · 2026Article
- Identification of protein precursor for thyroid hormone synthesis in basal chordate ascidian Styela clava.Nature communications · 2026Article
- Thyroidal expression of ER molecular chaperone GRP170 is required for efficient TSH-mediated thyroid hormone synthesis.JCI insight · 2025Article
- Acquisition of neural crest promoted thyroid evolution from chordate endostyle.Science advances · 2025Article
- A Genetically-Engineered Thyroid Gland Built for Selective Triiodothyronine Secretion.International journal of molecular sciences · 2025Article
- Clinical and molecular study of patients with thyroid dyshormogenesis and variants in theFrontiers in endocrinology · 2024Article
- Structural features of thyroglobulin linked to protein trafficking.Protein science : a publication of the Protein Society · 2023Article
- Perturbation of endoplasmic reticulum proteostasis triggers tissue injury in the thyroid gland.JCI insight · 2023Article
- Article
- Defective Thyroglobulin: Cell Biology of Disease.International journal of molecular sciences · 2022Review
- Article
- Thyroid hormone synthesis continues despite biallelic thyroglobulin mutation with cell death.JCI insight · 2021Article
- Review
- GWAS of thyroid stimulating hormone highlights pleiotropic effects and inverse association with thyroid cancer.Nature communications · 2020Article
- ERGO: Breaking Down the Wall between Human Health and Environmental Testing of Endocrine Disrupters.International journal of molecular sciences · 2020Review
- Article
- The structure of human thyroglobulin.Nature · 2020Article
Corrections and comments
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Authors and funding
11 authors at 5 institutions in 2 countries.
Funding
Abstract
Thyroid hormones modulate not only multiple functions in vertebrates (energy metabolism, central nervous system function, seasonal changes in physiology, and behavior) but also in some non-vertebrates where they control critical post-embryonic developmental transitions such as metamorphosis. Despite their obvious biological importance, the thyroid hormone precursor protein, thyroglobulin (Tg), has been experimentally investigated only in mammals. This may bias our view of how thyroid hormones are produced in other organisms. In this study we searched genomic databases and found Tg orthologs in all vertebrates including the sea lamprey (Petromyzon marinus). We cloned a full-size Tg coding sequence from western clawed frog (Xenopus tropicalis) and zebrafish (Danio rerio). Comparisons between the representative mammal, amphibian, teleost fish, and basal vertebrate indicate that all of the different domains of Tg, as well as Tg regional structure, are conserved throughout the vertebrates. Indeed, in Xenopus, zebrafish, and lamprey Tgs, key residues, including the hormonogenic tyrosines and the disulfide bond-forming cysteines critical for Tg function, are well conserved despite overall divergence of amino acid sequences. We uncovered upstream sequences that include start codons of zebrafish and Xenopus Tgs and experimentally proved that these are full-length secreted proteins, which are specifically recognized by antibodies against rat Tg. By contrast, we have not been able to find any orthologs of Tg among non-vertebrate species. Thus, Tg appears to be a novel protein elaborated as a single event at the base of vertebrates and virtually unchanged thereafter.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.