The ubiquitous transport activity known as system ASC is characterized by a preference for small neutral amino acids including alanine, serine, and cysteine. ASCT-1 and ASCT-2, recently cloned transporters exhibiting system ASC-like selectivity, are members of a major amino acid transporter family that includes a number of glutamate transporters. Here we show that ASCT1 functions as an electroneutral exchanger that mediates negligible net amino acid flux. The electrical currents previously shown to be associated with ASCT1-mediated transport result from activation of a thermodynamically uncoupled chloride conductance with permeation properties similar to those described for the glutamate transporter subfamily. Like glutamate transporters, ASCT1 activity requires extracellular Na+. However, unlike glutamate transporters, which mediate net flux and complete a transport cycle by countertransport of K+, ASCT-1 mediates only homo- and heteroexchange of amino acids and is insensitive to K+. The properties of ASCT-1 suggest that it may function to equilibrate different pools of neutral amino acids and provide a mechanism to link amino acid concentration gradients.