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Cited by 184Thyroid Disorders and TreatmentsEndoplasmic Reticulum Stress and DiseaseThyroid Cancer Diagnosis and Treatment

Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology

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Di Jeso, Bruno, Arvan, Peter·2016·Endocrine Reviews
DOI 10.1210/er.2015-1090PMC PMC4740344
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Abstract

Thyroglobulin (Tg) is a vertebrate secretory protein synthesized in the thyrocyte endoplasmic reticulum (ER), where it acquires N-linked glycosylation and conformational maturation (including formation of many disulfide bonds), leading to homodimerization. Its primary functions include iodide storage and thyroid hormonogenesis. Tg consists largely of repeating domains, and many tyrosyl residues in these domains become iodinated to form monoiodo- and diiodotyrosine, whereas only a small portion of Tg structure is dedicated to hormone formation. Interestingly, evolutionary ancestors, dependent upon thyroid hormone for development, synthesize thyroid hormones without the complete Tg protein architecture. Nevertheless, in all vertebrates, Tg follows a strict pattern of region I, II-III, and the cholinesterase-like (ChEL) domain. In vertebrates, Tg first undergoes intracellular transport through the secretory pathway, which requires the assistance of thyrocyte ER chaperones and oxidoreductases, as well as coordination of distinct regions of Tg, to achieve a native conformation. Curiously, regions II-III and ChEL behave as fully independent folding units that could function as successful secretory proteins by themselves. However, the large Tg region I (bearing the primary T4-forming site) is incompetent by itself for intracellular transport, requiring the downstream regions II-III and ChEL to complete its folding. A combination of nonsense mutations, frameshift mutations, splice site mutations, and missense mutations in Tg occurs spontaneously to cause congenital hypothyroidism and thyroidal ER stress. These Tg mutants are unable to achieve a native conformation within the ER, interfering with the efficiency of Tg maturation and export to the thyroid follicle lumen for iodide storage and hormonogenesis.

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  • TG is a protein dimer of 600 kDa with an unusually high number of ~60 disulfide bonds per monomer and 17 glycosylation sites, which confer remarkable stability and solubility to the protein.

    “TG, a protein dimer of 600 kDa, has an unusually high number of ~ 60 disulfide bonds per monomer and 17 glycosylation sites, which confer remarkable stability and solubility to the protein1,2,9.”

    From The structure of human thyroglobulin (2020) · cites this paper as [1]

    The Introduction reports about 60 disulfide bonds per Tg monomer, and section V identifies Tg as a homodimer, but gives its mass as 660 kDa rather than 600 kDa. The glycan-dependent oxidoreductase section reports 10–15 N-linked oligosaccharides per monomer, not 17; section VI says glycans generally increase protein solubility, but does not establish that the claimed structural features confer remarkable stability and solubility on Tg. (LLM, conf=0.90)

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Authors
Di Jeso, B., & Arvan, P.
Affiliations
  • Laboratorio di Patologia Generale (B.D.J.), Dipartimento di Scienze e Tecnologie Biologiche ed Ambientali, Università del Salento, 73100 Lecce, Italy;
  • University of Michigan (US)
ORCID
Arvan, Peter
Venue
Endocrine Reviews
Publisher
The Endocrine Society
Published
2015-11-23
Volume
37
Issue
1
Pages
2-36
ISSN
  • 0163-769X (ISSN-L)
  • 1945-7189
DOI
10.1210/er.2015-1090
PMC
PMC4740344
OpenAlex
W2173065406
Cited by
184
References
4
Citations by year
2026: 22 · 2025: 13 · 2024: 22 · 2023: 20 · 2022: 15 · 2021: 22 · 2020: 19 · 2019: 19 · 2018: 16 · 2017: 10 · 2016: 5 · 2014: 1
FWCI
1.51
Type
journal article
Language
en
Open access
Locations
  • Endocrine Reviews (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • AIRUS (submittedVersion)
Funders
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK040344)
Topics
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Cancer Diagnosis and Treatment
Keywords
thyroglobulin, N-glycosylation, disulfide bond formation, protein folding, congenital hypothyroidism, endoplasmic reticulum stress, secretory pathway
MeSH terms
Animals, Congenital Hypothyroidism, Endoplasmic Reticulum, Humans, Models, Biological, Models, Molecular, Mutation, Protein Conformation, Thyroglobulin, Thyroid Gland, Genetic Predisposition to Disease, Halogenation, Endoplasmic Reticulum Stress

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

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