Abstract
Voltage-gated Ca2+ channels (CaV) consist of four homologous but not identical concatenated transmembrane repeats (I-IV), each including six transmembrane segments: S1-S4 make up a voltage-sensing domain (VSD) while S5 and S6 constitute ¼ of the pore. CaV3.1 T-type channels are expressed in neurons and in the heart pacemaker cells, and belong to the family of low voltage activated CaV, exhibiting a relatively high open probability at hyperpolarized membrane potentials. To understand the molecular mechanisms underlying this unique voltage-dependent gating, we used voltage-clamp fluorometry to optically track the activation of each VSD in the human CaV3.1 expressed in Xenopus oocytes.
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