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Muscle Developmental Biology Lab (Sato Lab)
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The lab explores how muscle is built and how it carries out its function.

AboutAbout the lab
How is muscle built, and how does it move?
The Muscle Developmental Biology Lab studies how muscle is built and how it works.
For a muscle cell to contract, the proteins it has made must assemble correctly into myofibrils.
Another question the lab wants to answer is how the assembled proteins produce coordinated contraction.
Using the regulation of contraction by troponin and the function of myosin-binding proteins as clues, the lab investigates these mechanisms.
Key terms
- Myofibril
- The contractile apparatus inside a muscle cell, in which actin and myosin filaments are arranged in a regular pattern
- Troponin
- A protein that regulates muscle contraction in response to calcium
- Cofilin
- A protein that regulates the elongation and shortening of actin filaments. It functions across species and cell types
ResearchResearch themes
For a terminally differentiated muscle cell to contract, the proteins it has made must assemble correctly into myofibrils. The lab aims to clarify how this assembly process is controlled and how the assembled proteins produce coordinated contraction.
*Illustrative imageRegulation and evolution of muscle contraction
Movement by muscle is one of the things that make animals animals. Interested in how the mechanisms regulating contraction have changed during evolution and which parts have stayed the same, the lab showed that troponin in ascidians works as an accelerator type, and that troponin is not found in the adult muscles of echinoderms and hemichordates.
*Illustrative imageMyosin-binding proteins
Myosin-binding protein C (C-protein) is thought to gather myosin filaments and stabilize them. The lab determined the structure of this protein in mice and examined how it is expressed during muscle formation. It is now studying the protein's possible role as a regulator of contraction.
*Illustrative imageFermented feed and changes in muscle
Animals that eat fermented feed show improved physiological function. For pigs, an industry-academia team centered on Chiba University sells pork that takes advantage of this effect. To investigate how the effect influences muscle, the lab analyzes the expression of muscle proteins. It has become clear that muscle quality is changing.
*Illustrative imageHow the contractile apparatus forms
When muscle-type cofilin was increased or decreased in cultured muscle cells, actin filaments gathered abnormally and myofibrils failed to form properly. Mice lacking the gene also show severe damage to muscle fibers in the heart and skeletal muscle, so cofilin was found to be essential for the formation and maintenance of myofibrils.
MembersFaculty
- Associate ProfessorNaruki Sato
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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: “Muscle Tissue Capilary in Skeletal Muscle ( )” Berkshire Community College Bioscience Image Library / CC0 (cropped)
- Regulation and evolution of muscle contraction: “Microcosmus sabatieri” Sylvain Le Bris / CC BY-SA 4.0 (cropped)
- Myosin-binding proteins: “Protein Structure of human NDNF” Alpha Fold Team / CC BY 4.0 (cropped)
- Fermented feed and changes in muscle: “Pig farm Vampula 9” kallerna / CC BY-SA 4.0 (cropped)
- How the contractile apparatus forms: “Cells with nuclei in blue, energy factories in green and the actin cytoskeleton in red ( )” NIH Image Gallery from Bethesda, Maryland, USA / Public domain (cropped)
- Related lab (Neural Proteomics Lab (Terasaki Lab)): “Chk-UCH1-GFAP-20X-1” GerryShaw / CC BY-SA 4.0 (cropped)
- Related lab (Cell Function Regulation Lab (Matsura-Itakura Lab)): “Gram positive budding yeast cells” Microrao / CC BY-SA 4.0 (cropped)
- Related lab (Biological Molecular Motor Lab (Ito-Haraguchi Lab)): “Chara coralllina var. kyusyuensis” Show_ryu / CC BY-SA 3.0 (cropped)
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