Ezrin mediates tethering of the gamma-aminobutyric acid transporter GAT1 to actin filaments via a C-terminal PDZ-interacting domain.

ABSTRACT: A high density of neurotransmitter transporters on axons and presynaptic boutons is required for the efficient clearance of neurotransmitters from the synapse. Therefore, regulators of transporter trafficking (insertion, retrieval, and confinement) can play an important role in maintaining the transporter density necessary for effective function. We determined the interactions that confine GAT1 at the membrane by investigating the lateral mobility of GAT1-yellow fluorescent protein-8 (YFP8) expressed in neuroblastoma 2a cells. Through fluorescence recovery after photobleaching, we found that a significant fraction ( approximately 50%) of membrane-localized GAT1 is immobile on the time scale investigated ( approximately 150 s). The mobility of the transporter can be increased by depolymeriz

SUBMITTER: Imoukhuede PI 

PROVIDER: S-EPMC2711277 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature