HOME arrowResearch arrowResearchers List arrowTSUKAMOTO, Hisao

Researchers detail

Assistant Professor


TEL: 0564-55-7453
Mail: tsukamoh_at_ims.ac.jp (Please replace the "_at_" with @ )
Affiliation laboratory:
Location: Myoudaiji, Main Office Bldg. Room309


Life and Coordination-Complex Molecular Science, Biomolecular Sensing


2001 B.S. Kyoto University 
2006 Ph.D.  Kyoto University
2006 Visiting Researcher, Osaka City University    
2006 Research fellow, Kyoto University    
2007 Postdoctoral fellow, Osaka City University    
2007 JSPS fellow (PD)    
2009 Oregon Health & Science University, Visiting Scientist    
2010 Oregon Health & Science University, Postdoctoral Trainee    
2011 JSPS fellow for Research Abroad    
2011 Research Assistant Professor, Institute for Molecular Science    
2014 Assistant Professor, Institute for Molecular Science   


2010 Reseach Fellowship, The Uehara Memolial Foundation    
2013 Presentation award, The Biophysical Society of Japan -Chubu-   

Specialized field

Molecular Physiology, Biophysics

Main research themes

Investigation of molecular mechanisms underlying functional differences in membrane proteins.
kewords biochemistry, molecular physiology, photobiology

Selected Publications

  1. H. Tsukamoto, D. L. Farrens, M. Koyanagi, A. Terakita. The magnitude of the light-induced conformational change in different rhodopsins correlates with their ability to activate G proteins. Journal of Biological Chemistry 284, 20676-20683 (2009).
  2. H. Tsukamoto, A. Sinha, M. DeWitt, D. L. Farrens. Monomeric rhodopsin is theminimal functional unit required for arrestin binding. Journal of Molecular Biology 399, 501-511 (2010).
  3. H. Tsukamoto and A. Terakita. Diversity and functional properties of bistable pigments. Photochemical & Photobiological Sciences 9, 1435-1443 (2010).
  4. H. Tsukamoto, I. Szundi, J. W. Lewis, D. L. Farrens, D. S. Kliger. Rhodopsin in nanodiscs has native membrane-like photointermediates. Biochemistry 50, 5086-5091 (2011).
  5. H. Tsukamoto, D. L. Farrens. A constitutively activating mutation alters the  dynamics of a key conformational change in a ligand-free G protein-coupledreceptor. Journal of Biological Chemistry, 288, 28207-28216 (2013).