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Structural models of mitochondrial uncoupling proteins obtained in DPC micelles are not functionally relevant
Author(s) -
Piel Mathilde S.,
Masscheleyn Sandrine,
Bouillaud Frédéric,
Moncoq Karine,
Miroux Bruno
Publication year - 2021
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.15629
Subject(s) - thermogenin , biochemistry , chemistry , mutant , uncoupling protein , saccharomyces cerevisiae , context (archaeology) , mitochondrion , inner mitochondrial membrane , fatty acid , biophysics , yeast , biology , thermogenesis , gene , brown adipose tissue , paleontology , adipose tissue
The mitochondrial uncoupling protein 1 (UCP1) is responsible for nonshivering thermogenesis in mammals. NMR experiments in DPC micelles identified two crucial residues K56 and K269 for fatty acid binding and UCP1 activation. Using mitochondrial respiration, we revisit those residues in a physiological context. We show that mutation of K56 and K269 does not alter the uncoupling activity of UCP1 supporting the damaging properties of DPC on UCP1 and related carriers.