Homodimeric intrinsic membrane proteins. Identification and modulation of interactions between mitochondrial transporter (carrier) subunits.

ABSTRACT: Transporter (carrier) proteins of the inner mitochondrial membrane link metabolic pathways within the matrix and the cytosol with transport/exchange of metabolites and inorganic ions. Their strict control of these fluxes is required for oxidative phosphorylation. Understanding the ternary complex transport mechanism with which most of these transporters function requires an accounting of the number and interactions of their subunits. The phosphate transporter (PTP, Mir1p) subunit readily forms homodimers with intersubunit affinities changeable by mutations. Cys28, likely at the subunit interface, is a site for mutations yielding transport inhibition or a channel-like transport mode. Such mutations yield a small increase or decrease in affinity between the subunits. The PTP inhibitor N-ethy

SUBMITTER: Wohlrab H 

PROVIDER: S-EPMC2843762 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature