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Biophys J, July 2002, p. 206-218, Vol. 83, No. 1
Division of Biology 156-29, California Institute of Technology, Pasadena, California 91125 USA
The mammalian serotonin transporters rSERT or hSERT were
expressed in oocytes and labeled with sulforhodamine-MTS. The
endogenous Cys-109 residue contributes most of the signal, and the
labeled transporter shows normal function. The SERT fluorescence
decreases in the presence of 5-HT and also depends on the inorganic
substrates of SERT. The fluorescence also increases with membrane
depolarization. During voltage-jump experiments, fluorescence
relaxations show little inactivation or history dependence. The
fluorescence signal has a voltage dependence similar to that of the
prepriming step of the previously described voltage-dependent transient
current. However, the fluorescence relaxations are the fastest
voltage-dependent events yet studied at SERT; their time constants of
~8-30 ms are severalfold faster than the prepriming or inactivation
phases of the transient currents. These fluorescence signals are
interpreted within the framework of the gate-lumen-gate model. The
signals may monitor initial events at the outer gate.
Biophys J, July 2002, p. 206-218, Vol. 83, No. 1
© 2002 by the Biophysical Society 0006-3495/02/07/206/13 $2.00
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