Abstract
The structure/function relationship in the uncoupling proteins (UCP) is reviewed, stressing UCP from brown adipose tissue (UCP1) since, so far, nearly no biochemistry is known for the UCP variants UCP2, UCP3, and UCP4. The transport for H+ and Cl- and its dependence on fatty acids in reconstituted vesicles is described. The inhibition and binding of nucleotides to UCP1, in particular, the pH dependence and two-stage binding are analyzed. A model for the role of fatty acid in H+ transport is shown. The role of specific residues in UCP1 is analyzed by directed mutagenesis in a yeast expression system. The different regulation by the cellular energy potential of UCP1 versus UCP3 is discussed.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adipose Tissue, Brown / metabolism*
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Amino Acid Sequence
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Animals
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Biological Transport
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Carrier Proteins / genetics
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Carrier Proteins / metabolism*
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Energy Metabolism* / physiology
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Ion Channels
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Membrane Proteins / genetics
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Membrane Proteins / metabolism*
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Membrane Transport Proteins*
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Mitochondria / metabolism*
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Mitochondrial Proteins*
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Mitochondrial Uncoupling Proteins
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Molecular Sequence Data
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Mutagenesis
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Nucleotides / metabolism
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Proteins
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Uncoupling Agents / metabolism*
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Uncoupling Protein 1
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Uncoupling Protein 2
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Uncoupling Protein 3
Substances
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Carrier Proteins
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Ion Channels
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Membrane Proteins
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Membrane Transport Proteins
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Mitochondrial Proteins
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Mitochondrial Uncoupling Proteins
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Nucleotides
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Proteins
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SLC25A27 protein, human
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UCP1 protein, human
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UCP2 protein, human
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UCP3 protein, human
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Uncoupling Agents
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Uncoupling Protein 1
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Uncoupling Protein 2
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Uncoupling Protein 3