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Endogenous mutations in human uncoupling protein 3 alter its functional properties
Author(s) -
Brown Angela M.,
Dolan Joseph W.,
Willi Steven M.,
Garvey W.Timothy,
Argyropoulos George
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01708-1
Subject(s) - uncoupling protein , ucp3 , oxidative phosphorylation , mutation , endogeny , uncoupling agents , phosphorylation , microbiology and biotechnology , biology , transmembrane protein , mitochondrion , inner mitochondrial membrane , yeast , biochemistry , gene , chemistry , receptor , adipose tissue , brown adipose tissue
Human uncoupling protein 3 (UCP3) is a mitochondrial transmembrane carrier that uncouples oxidative phosphorylation and is a candidate gene for obesity. Expression of native human UCP3 mutations in yeast showed complete loss (R70W), significant reduction (R143X), or no effect (V102I and IVS6+1G>A) on the uncoupling activity of UCP3. It is concluded that certain mutations in UCP3 alter its functional impact on membrane potential (Δ Ψ ), possibly conferring susceptibility to develop metabolic diseases.