Abstract
We investigated the role of cysteine residues in activity and localization of the NHE1 isoform of the Na+/H+exchanger. Each of the nine cysteine residues was mutated to serine or arginine. Mutation of the first serine (amino acid number 9) and serine number six (amino acid number 477) resulted in dramatic decreases in detectable activity of the Na+/H+exchanger when transfected into AP-1 cells. Some other mutations resulted in minor decreases in activity of the protein. Confocal and light microscopy of mutant cells with decreased activity showed that the antiporter protein was mostly retained in an intracellular compartment which colocalized with the medial-Golgi cisternae. Smaller amounts of active protein still remained targeted to the plasma membrane in these mutants. Treatment of wild-type cells with DTT also caused the retention of the Na+/H+exchanger to the same intracellular compartment. The results suggest that cysteines play an important role in intracellular folding and trafficking of the Na+/H+exchanger.
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