Hirohide Takahashi Email & Phone Number

Groton, Connecticut, United States

Greater Nashville Area, Tn

I am currently working on the structural biology of Membrane proteins using cryoEM. I have been purifying and characterizing the molecular structure of membrane proteins including inositol 1,4,5-trisphosphate (IP3) receptors, Volume-regulated anion channel (VRAC) and Inward-rectifier potassium channels (Kir) for the structural analysis by cryo-EM. I have also been working on a research project while training a research associate.

I investigated molecular dynamics of proteins using High-Speed force microscopy (HS-FS), which enables analysis of protein dynamics at sub-milli second time frame. By using HS-FS, I studied unfolding of spectrin, which is a cytoskeletal protein forming filamentous network on the inner plasma membrane. I identified that spectrin unwinds in unfolding process.

Marseille Area, France

I investigated molecular dynamics of proteins using High-Speed atomic force microscopy (HS-AFM), which enables analysis of protein dynamics at sub-milli second time frame. I developed a temperature-controlled device for HS-AFM. Using this device, I succeeded in real-time imaging of lipid phase transition in a temperature-changing manner.

Cambridge, United Kingdom

During my postdoctoral period at the Department of Pharmacology at the University of Cambridge, I studied the molecular structure of vesicle trafficking proteins such as synaptotagmin, and endosomal sorting complexes required for transport (ESCRT) proteins using force spectroscopy. Synaptotagmin is a trigger protein that promotes synaptic vesicle fusion upon calcium ion influx into the presynaptic cytoplasm. I demonstrated that synaptotagmin interacts with the presynaptic membrane even in the absence of calcium, albeit much weaker. In another study, I investigated how mono-ubiquitinated cargo molecules are recruited to the endosomal sorting complex required for transport (ESCRT) machinery that mediates the turnover of integral membrane proteins. We showed that only ESCRT-0, among the three different components of the ESCRT machinery, can associate stably with the mono-ubiquitinated cargo molecules within the lipid bilayer. Moreover, my studies revealed that both Hrs and STAM, ubiquitin binding subunits of ESCRT-0, are necessary for recruiting ubiquitinated protein.

Doctor Of Philosophy - Phd, Life Science

During my doctoral training, I developed a site-specific attachment of biomolecules to a solid substrate surface, enabling measurement.

Bachelor Of Science - Bs, Biology And Geoscience