ArticleThe Journal of biological chemistry2011
Repeat motif-containing regions within thyroglobulin.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Substrate for Thyroid Hormone Synthesis: Biochemistry, Evolution, and Physiology.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- 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
- Article
- The structure of human thyroglobulin.Nature · 2020Article
- The role of thyroglobulin in thyroid hormonogenesis.Nature reviews. Endocrinology · 2019Review
- Thyroglobulin Represents a Novel Molecular Architecture of Vertebrates.The Journal of biological chemistry · 2016Article
- Thyroglobulin From Molecular and Cellular Biology to Clinical Endocrinology.Endocrine reviews · 2016Review
- Transient covalent interactions of newly synthesized thyroglobulin with oxidoreductases of the endoplasmic reticulum.The Journal of biological chemistry · 2014Article
- Congenital hypothyroidism mutations affect common folding and trafficking in the α/β-hydrolase fold proteins.The FEBS journal · 2012Article
- GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.Biochimica et biophysica acta · 2012Review
- Maturation of thyroglobulin protein region I.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 2 countries.
Funding
Abstract
Thyroglobulin (precursor for thyroid hormone synthesis) is a large secreted glycoprotein comprising contiguous region I (multiple type-1 repeating units engaging the first ∼1,191 residues, followed by a ∼245-residue hinge region), regions II-III (multiple type-2 and 3 repeating units, comprising ∼720 residues), and the C-terminal cholinesterase-like (ChEL) domain (∼570 residues). A signal peptide attached to ChEL makes an independent secretory protein that binds to I-II-III, stabilizing it and rescuing the secretion of I-II-III that would otherwise be trapped in the endoplasmic reticulum (ER). In this study, we found that a signal peptide attached to regions II-III also makes for an efficient secretory protein that neither demonstrably interacts nor has its secretion enhanced by the presence of secretory ChEL. By contrast, region I, either with or without the hinge region, cannot be secreted on its own and remains in the ER where it is bound to ER chaperones BiP and GRP94. Whereas ChEL can rescue secretion of I-II-III, it can rescue I-II only very weakly, and region I not at all. Yet, ChEL begins to rescue region I in cells that also co-express secretory II-III. The data suggest that conformational maturation of region I is a limiting step in the thyroglobulin maturation process, and this step is facilitated by the presence of both regions II-III and ChEL. Mutations causing hypothyroidism might induce solely local/regional misfolding or may interfere more globally by impeding interactions between regions that are required for thyroglobulin secretion.
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Registered trials
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