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Insertion Of Tetracysteine Motifs Into Dopamine Transporter Extracellular Domains, Deanna M. Navaroli, Haley E. Melikian
Insertion Of Tetracysteine Motifs Into Dopamine Transporter Extracellular Domains, Deanna M. Navaroli, Haley E. Melikian
Haley Melikian
The neuronal dopamine transporter (DAT) is a major determinant of extracellular dopamine (DA) levels and is the primary target for a variety of addictive and therapeutic psychoactive drugs. DAT is acutely regulated by protein kinase C (PKC) activation and amphetamine exposure, both of which modulate DAT surface expression by endocytic trafficking. In order to use live imaging approaches to study DAT endocytosis, methods are needed to exclusively label the DAT surface pool. The use of membrane impermeant, sulfonated biarsenic dyes holds potential as one such approach, and requires introduction of an extracellular tetracysteine motif (tetraCys; CCPGCC) to facilitate dye binding. …
The Plasma Membrane-Associated Gtpase Rin Interacts With The Dopamine Transporter And Is Required For Protein Kinase C-Regulated Dopamine Transporter Trafficking, Deanna M. Navaroli, Zachary H. Stevens, Zeljko Uzelac, Luke Gabriel, Michael J. King, Lawrence M. Lifshitz, Harald H. Sitte, Haley E. Melikian
The Plasma Membrane-Associated Gtpase Rin Interacts With The Dopamine Transporter And Is Required For Protein Kinase C-Regulated Dopamine Transporter Trafficking, Deanna M. Navaroli, Zachary H. Stevens, Zeljko Uzelac, Luke Gabriel, Michael J. King, Lawrence M. Lifshitz, Harald H. Sitte, Haley E. Melikian
Haley Melikian
Dopaminergic signaling and plasticity are essential to numerous CNS functions and pathologies, including movement, cognition, and addiction. The amphetamine- and cocaine-sensitive dopamine (DA) transporter (DAT) tightly controls extracellular DA concentrations and half-life. DAT function and surface expression are not static but are dynamically modulated by membrane trafficking. We recently demonstrated that the DAT C terminus encodes a PKC-sensitive internalization signal that also suppresses basal DAT endocytosis. However, the cellular machinery governing regulated DAT trafficking is not well defined. In work presented here, we identified the Ras-like GTPase, Rin (for Ras-like in neurons) (Rit2), as a protein that interacts with the …