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• W2097789207 abstract "Thyroid hormonogenesis requires secretion of thyroglobulin, a protein comprising Cys-rich regions I, II, and III (referred to collectively as region I-II-III) followed by a cholinesterase-like (ChEL) domain. Secretion of mature thyroglobulin requires extensive folding and glycosylation in the ER. Multiple reports have linked mutations in the ChEL domain to congenital hypothyroidism in humans and rodents; these mutations block thyroglobulin from exiting the ER and induce ER stress. We report that, in a cell-based system, mutations in the ChEL domain impaired folding of thyroglobulin region I-II-III. Truncated thyroglobulin devoid of the ChEL domain was incompetent for cellular export; however, a recombinant ChEL protein (“secretory ChEL”) was secreted efficiently. Coexpression of secretory ChEL with truncated thyroglobulin increased intracellular folding, promoted oxidative maturation, and facilitated secretion of region I-II-III, indicating that the ChEL domain may function as an intramolecular chaperone. Additionally, we found that the I-II-III peptide was cosecreted and physically associated with secretory ChEL. A functional ChEL domain engineered to be retained intracellularly triggered oxidative maturation of I-II-III but coretained I-II-III, indicating that the ChEL domain may also function as a molecular escort. These insights into the role of the ChEL domain may represent potential therapeutic targets in the treatment of congenital hypothyroidism." @default.
• W2097789207 created "2016-06-24" @default.
• W2097789207 creator A5007645545 @default.
• W2097789207 creator A5072170846 @default.
• W2097789207 creator A5085109740 @default.
• W2097789207 date "2008-08-01" @default.
• W2097789207 modified "2023-09-27" @default.
• W2097789207 title "The cholinesterase-like domain of thyroglobulin functions as an intramolecular chaperone" @default.
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• W2097789207 doi "https://doi.org/10.1172/jci35164" @default.
• W2097789207 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2441857" @default.
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