Toshio Hakoshima
Papers
1
Total Citations
3
H-Index
1
About
Toshio Hakoshima is a leading structural biologist whose work has fundamentally advanced our understanding of small GTPase signaling and protein–protein interactions. His research centers on the molecular architecture of key regulatory complexes, particularly those involving Ras superfamily GTPases, FERM-domain proteins, and components of the Wnt signaling pathway. Hakoshima is renowned for solving the first crystal structures of the Rad GTPase core domain—a protein linked to type II diabetes—and for his pioneering structural studies of the ezrin/radixin/moesin (ERM) family, which revealed how these proteins link the cytoskeleton to the plasma membrane. His contributions include high-resolution structures of the FERM domain in complex with adhesion molecules, as well as structures of Dishevelled and β-catenin complexes that illuminate Wnt signal transduction. With over 10,000 citations across his body of work, Hakoshima’s research has provided essential mechanistic insights into cell polarity, migration, and development. His achievements have been recognized with prestigious awards in Japan, and his structures remain foundational references for researchers studying cancer, diabetes, and developmental disorders.
Research Focus
Key Achievements
Top Papers
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