Background: Secretory proteins acquire their native three-dimensional conformation through repeated brief interactions with ER chaperones and oxidoreductases. Results: We have captured and defined previously-unidentified disulfide adducts of newly-synthesized thyroglobulin with ERp72 and CaBP1/P5. Conclusion: Multiple oxidoreductases simultaneously engage thyroglobulin during its early folding in the ER. Significance: Distinct chaperone/oxidoreductase partners coordinately engage this multi-domain secretory protein to promote its advancement to the native state.
Transient Covalent Interactions of Newly-Synthesized Thyroglobulin with Oxidoreductases of the Endoplasmic Reticulum
DI JESO, Bruno
Primo
Membro del Collaboration Group
;TREGLIA, Antonella Sonia;LOFRUMENTO, Dario DomenicoMembro del Collaboration Group
;NICOLARDI, Giuseppe;
2014-01-01
Abstract
Background: Secretory proteins acquire their native three-dimensional conformation through repeated brief interactions with ER chaperones and oxidoreductases. Results: We have captured and defined previously-unidentified disulfide adducts of newly-synthesized thyroglobulin with ERp72 and CaBP1/P5. Conclusion: Multiple oxidoreductases simultaneously engage thyroglobulin during its early folding in the ER. Significance: Distinct chaperone/oxidoreductase partners coordinately engage this multi-domain secretory protein to promote its advancement to the native state.File in questo prodotto:
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