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Trans-scale Structural Life Science Lab
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A lab that explores how cells maintain protein quality control, from molecular structure to the cellular level.
AboutAbout the lab
Unraveling protein quality control through both structure and cells
The Trans-scale Structural Life Science Lab studies how cells maintain protein quality, from the level of molecular structure to the level of the cell.
Because proteins can function only after folding into the correct three-dimensional structure, cells have mechanisms that help proteins fold properly and mechanisms that remove those that fail to do so.
The lab investigates how these two mechanisms work, using methods such as structural biology, biochemistry, and cell biology.
On the lab's website, it is presented under the name "Inaba Lab."
Key terms
- Endoplasmic reticulum (ER)
- An organelle in the cell. The compartment where secretory proteins and membrane proteins are synthesized
- Disulfide bond
- A sulfur-sulfur bond formed between two cysteine residues. It stabilizes the three-dimensional structure of proteins
- ER-associated degradation
- A mechanism that sends proteins that failed to fold correctly back to the cytosol and degrades them
- ERp44
- A protein that, in the Golgi apparatus, captures proteins that should be returned to the ER and sends them back
NewsLab news
Students won the Outstanding Presentation Award and the Best Poster Award at the Medical Institute of Bioregulation retreat
Review article on ERp44 and ERGIC-53 published in the Journal of Biochemistry
Review article comparing SERCA2 and SPCA1 published in Biochemical Journal
Assistant Professor Amagai and colleagues discovered a link between zinc and redox state in the ER; the paper was published in Nature Communications
ResearchResearch themes
The lab studies the protein quality control mechanisms that cells possess, from the level of molecular structure to the level of the cell. By combining methods from structural biology, biochemistry, proteomics, and cell biology, it investigates how the mechanisms involved in quality control work.
*Illustrative imageDisulfide Bond Formation in the Endoplasmic Reticulum
The mammalian endoplasmic reticulum (ER) contains many PDI family enzymes, and there are also multiple pathways for forming disulfide bonds. These are thought to form a complex network, and the challenge is to analyze its details and the role of each pathway comprehensively.
*Illustrative imageDegradation of Misfolded Proteins
The ER enzyme ERdj5 is thought to reduce incorrect disulfide bonds in misfolded proteins, making them easier to degrade. The lab has solved the crystal structure of ERdj5 and proposed a model for how this ER-associated degradation works.
*Illustrative imageRetrieval from the Golgi Apparatus to the ER
In the Golgi apparatus, ERp44 captures proteins that should be returned to the ER and sends them back. It is known to sense the pH difference between the ER and the Golgi apparatus, and to switch between binding and dissociating from its partners by opening and closing its tail region.
*Illustrative imageMaintaining Metal Ion Concentrations
Many proteins bind metal ions, and organelles have mechanisms that tightly regulate metal ion concentrations. The lab aims to elucidate this kind of network that maintains protein homeostasis.
MembersFaculty
The lab's members consist of faculty, technical staff, and doctoral and master's students.As of 2026
- Senior ProfessorKenji Inaba
- Associate ProfessorSatoshi Watanabe
- Assistant ProfessorYuta Amagai
- Assistant ProfessorShohei Fujii
- Project Associate ProfessorHiroshi Kadokura
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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: “XBio illustration – Endoplasmic Reticulum” explorebiology / CC BY 4.0 (cropped)
- Disulfide Bond Formation in the Endoplasmic Reticulum: “C17orf58 protein (UPF0450) structure with AlphaFold” Luyu9927 / CC BY 4.0 (cropped)
- Degradation of Misfolded Proteins: “Ubiquitin cartoon” en:User:Rogerdodd / Public domain (cropped)
- Retrieval from the Golgi Apparatus to the ER: “Golgi apparatus 2 -- Smart-Servier” Laboratoires Servier / CC BY-SA 3.0 (cropped)
- Maintaining Metal Ion Concentrations: “Zinc (Element - 30)” James St. John / CC BY 2.0 (cropped)
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