René Caballero-Florán is a research investigator in Paul Jenkins’ lab in the Department of Pharmacology at the University of Michigan. He has extensive research experience in pharmacology, with expertise in electrophysiology, biophysics and neuroscience. His research interests include performing integrative research to learn about the physiology of synapse formation, how genetic changes affect neuronal communication, and how this leads to neurological disorders. During his undergraduate studies, Caballero-Florán investigated the mechanisms of action of cannabinoids and opioids with the goal of developing new treatments for Parkinson’s. During research for his master’s degree (awarded with honors), he discovered that the dimerization of cannabinoid and dopamine receptors causes changes in signaling pathways that modulate neurotransmitter release in Parkinson’s disease. In addition, he worked in clinical research studies for the pharmaceutical industry to evaluate the efficacy, safety and pharmacokinetics of new drugs. During his doctorate, he performed in vivo electrophysiological recordings to predict changes in neuronal plasticity by measuring neurotransmitter release evoked by electrical pulses, allowing him to start new lines of research in his former lab. As a postdoctoral fellow, he enhanced electrophysiology practices and combined them with genetic and molecular biology techniques to describe the pathophysiological mechanisms involved in neurological and psychiatric disorders.

Principal Investigator: Paul Jenkins

Fellow: Kristina Aksovski

Undergraduate Fellow Project: Autism-associated polymorphisms in NaV1.2 channels alter their electrophysiological properties, impacting neuronal excitability
SCN2A and ANK2 are strong risk genes for autism. The voltage-gated sodium channel NaV1.2 (product of SCN2A) is located at the dendrites in mature neurons, where it promotes action potential backpropagation necessary for normal synaptic function. Ankyrin-B, (product of the gene ANK2) is an intracellular scaffolding protein that is highly enriched in the soma and distal dendrites. We recently discovered that ankyrin-B is the dendritic scaffold for NaV1.2, and that deleting ankyrin-B significantly reduced NaV1.2 dendritic localization. While we have identified disease-associated variants within the binding interface between the two proteins, not all the variants in the interface influenced the binding affinity of NaV1.2 to ankyrin-B, suggesting that they may influence channel function in other ways. Our research project involves performing whole-cell electrophysiological voltage-clamp recordings in mammalian cells to compare the biophysical properties of wild-type NaV1.2 channels to those of NaV1.2 channels with autism-associated polymorphisms that do not disrupt the binding to ankyrin-B. This is critical because changes in ion channel electrophysiological properties can influence neuronal excitability and synaptic function, and thus can contribute to the etiology of autism.