Structural models of mitochondrial uncoupling proteins obtained in DPC micelles are not functionally relevant | Zendy

Piel Mathilde S. | Zendy; Masscheleyn Sandrine | Zendy; Bouillaud Frédéric | Zendy; Moncoq Karine | Zendy; Miroux Bruno | Zendy

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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) - uncoupling protein , micelle , biophysics , chemistry , microbiology and biotechnology , mitochondrion , biochemistry , biology , adipose tissue , brown adipose tissue , aqueous solution

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.

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