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Medical Biochemistry Lab
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A lab that explores the mechanisms of cancer and immunity through protein ubiquitination.
AboutAbout the lab
Understanding disease through how proteins are degraded
The lab studies the mechanisms of protein degradation, centered on ubiquitination, a post-translational modification of proteins.
Ubiquitination is involved in many bodily functions, including cancer, immunity, intracellular signal transduction, and neuronal differentiation.
The lab conducts basic research to identify the enzymes responsible for ubiquitination and characterize their functions, as well as research that clarifies links to disease in order to lead to prevention and treatment.
Key terms
- Ubiquitination
- A reaction that attaches the small protein ubiquitin to other proteins. It acts as a marker for degradation, among other roles.
- Post-translational modification
- A mechanism in which chemical tags are added to a protein after it has been made, changing its function.
- Ubiquitin ligase
- An enzyme that recognizes the target protein to which ubiquitin is to be attached and carries out ubiquitination.
NewsLab news
Collaborative study on how RNA derived from gut bacteria suppresses colorectal cancer published in Cell Reports
Paper on a new degradation pathway of PPM1D, a cancer-promoting enzyme, published in J Biomed Sci
Review on neurological and inflammatory diseases and tryptophan derivatives published in Eur J Cell Biol
ResearchResearch themes
The lab investigates, down to the level of individual enzymes, how ubiquitination determines protein degradation. It aims to clarify how ubiquitination and phosphorylation contribute to cancer, immune diseases, and neurological diseases, and to translate this into prevention and treatment.
*Illustrative imageUbiquitination and protein degradation
Proteins inside the cell are tagged with ubiquitin, recognized by a molecular machine called the proteasome, and degraded. The lab studies how this mechanism regulates processes such as intracellular signal transduction and the cell cycle.
*Illustrative imageDiversity of ubiquitin ligases
Ubiquitin ligases, the enzymes that determine which proteins receive ubiquitin, come in many types with different structures. The lab identifies such enzymes involved in ubiquitination and investigates how they function.
*Illustrative imageUbiquitination and phosphorylation in disease
The lab investigates how ubiquitination and phosphorylation are involved in cancer, immune diseases, and neurological diseases, and pursues research toward prevention and treatment.
MembersFaculty
The lab's members consist of faculty, administrative assistants, technical assistants, master's and undergraduate students, and members who join the research from other departments.As of 2026
- ProfessorShigetsugu Hatakeyama
- LecturerTakeshi Kondo
- Assistant ProfessorTadasuke Tsukiyama
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Report an errorAbout the images
The top and research theme images are illustrative and were not taken at the lab. They are cropped from Wikimedia Commons images. Cropped CC BY-SA images are provided under the same CC BY-SA license as the original (version shown on each line).
- Top image: “Ubiquitin 1UBQ surface” Thomas Splettstoesser (www.scistyle.com) / CC0 (cropped)
- Ubiquitination and protein degradation: “26S proteasome structure” FridoFoe / CC BY-SA 3.0 (cropped)
- Diversity of ubiquitin ligases: “PDB 1ldj EBI” Jawahar Swaminathan and MSD staff at the European Bioinformatics Institute / Public domain (cropped)
- Ubiquitination and phosphorylation in disease: “Multicolor fluorescence image of living HeLa cells” 8x57is / CC BY-SA 4.0 (cropped)
- Related lab (細胞生理学): “FPbeachTsien” Nathan Shaner / CC BY-SA 3.0 (cropped)
- Related lab (神経生理学): “Cortical neurons” Luisa Demarchi, Ilaria Bertocchi, Alessandra Oberto / CC BY-SA 4.0 (cropped)
- Related lab (神経薬理学): “Diphenhydramine 3D 2aot” Fvasconcellos (talk · contribs) / Public domain (cropped)
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