Takanori Otomo, PhD

Associate Professor
Department of Integrative Structural and Computational Biology
California Campus

Scripps Research Joint Appointments

Faculty, Graduate Program

Research Focus

Structural Biology of Autophagy

Research in the Otomo laboratory is focused on elucidation of the structural and functional bases of proteins involved in autophagy. Autophagy is an degradation-recycling mechanism that plays important roles in energy homeostasis and damage control in eukaryotic cells. The key feature of autophagy is the utilization of membrane-bound vesicles called autophagosomes for sequestration of aberrant proteins and organelles in the cytoplasm into lysosomes. We aim to reveal the mechanistic bases of steps during autophagosome formation using a combination of structural methods and biochemistry. Knowledges on mechanisms of autophagy emerging from our work are expected to advance understanding of autophagy-involved processes and human diseases such as aging, cancer, neurodegeneration, and infections.


Ph.D., Osaka University, 2001

Professional Experience

2013-2018 Assistant Professor, Integrative Structural and Computational Biology (ISCB), Scripps Research
2007-2012 Assistant Professor, Molecular Biology, Scripps Research

Selected References

All Publications

Otomo, C., Metlagel, Z., Takaesu, G., and Otomo, T. Structure of the human ATG12~ATG5 conjugate required for LC3 lipidation in autophagy. Nature Structural and Molecular Biology 2012 doi:10.1038/nsmb.2431

Otomo, T., Tomchick, D.R., Otomo, C., Machius, M., and Rosen, M.K. Crystal structure of the Formin mDia1 in autoinhibited conformation. PLoS One. 5:e12896, 2010

Otomo, T., Otomo, C., Tomchick, D.R., Machius, M., and Rosen, M.K. Structural basis of Rho GTPase-mediated activation of the formin mDia1. Molecular Cell 18:273-81, 2005

Otomo, T., Tomchick, D.R., Otomo, C., Panchal, S.C., Machius, M., and Rosen, M.K. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433:488-94, 2005.