Susumu Tomita, PhD

Professor of Cellular And Molecular Physiology

Departments & Organizations

Cellular & Molecular Physiology: Graduate Program in Cellular and Molecular Physiology

Interdepartmental Neuroscience Program

Kavli Institute for Neuroscience

Office of Student Research

Program in Cellular Neuroscience, Neurodegeneration and Repair

Yale Combined Program in the Biological and Biomedical Sciences (BBS): Molecular Medicine, Pharmacology, and Physiology: Ion Channels, Pumps and Transporters; Neurobiology, Neural Networks and Neuropharmacology; Protein Sorting and Trafficking; Receptors and Signal Transduction | Neuroscience: Molecular/Cellular Neuroscience

Education & Training

PhD University of Tokyo (2000)
Postdoctoral fellowship UCSF

Honors & Recognition

  • Alfred P. Sloan Research Fellowship AwardAlfred P. Sloan Research Foundation (2007)

  • NARSAD Young Investigator AwardNARSAD (2007)

  • Klingenstein Fellowship Awards In The NeurosciencesThe Esher and Joseph Klingenstein Foundation (2006)

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Contact Info

Susumu Tomita, PhD
Mailing Address
Department of Cellular & Molecular PhysiologyPO Box 208026
333 Cedar Street

New Haven, CT 06520-8026

Tomita Lab.

Research Image 2

A, TARPs consist of four isoforms (stargazin, g -3, g -4, and g -8), which show distinct expression patterns in the brain . B, TARPs (green) colocalize with the glutamatergic markers AMPA receptors (red)(left panel), but not with the GABAergic marker GAD65 (red)(right panel). C, TARPs both modulate trafficking of AMPA receptors to the synapses and control the gating and pharmacology of the channel. Oocytes injected with GluR1 alone are more sensitive to glutamate (Glu) than to kainate (KA). D, AMPA receptor subunits GluR1, GluR2 and GluR4 co-immunoprecipitate with stargazin (STG) in brain extracts from +/stg mice (+/-), but not in extracts from stg/stg mice (-/-). E, TARPs stabilize AMPA receptors at synapses through its C-terminal PDZ domain binding motif.