F.-Ulrich Hartl Receives Prestigious Japanese Science Award

F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry, is receiving this year’s “Keio Medical Science Prize” for his work in elucidating the mechanisms of protein folding mediated by molecular chaperones and beyond.

This year’s Japanese science prize, the “Keio Medical Science Prize,” will be awarded to F.-Ulrich Hartl, for his “elucidation of the mechanisms of protein folding mediated by molecular chaperones and beyond.” Awarded by Japan’s oldest private university, the prize recognizes his outstanding contributions to the field of life sciences and comes with a cash award of 10 million Japanese yen. The ceremony will take place on November 26 at Keio University in Tokyo, Japan.

Proteins are the building blocks of life. They are composed of amino acids, their basic building units. In order for proteins to perform their specific, vital functions, they must be folded correctly. For a long time, scientists assumed that newly synthesized proteins folded spontaneously based solely on the information encoded in their amino acid sequences.

However, how newly synthesized proteins achieve their correct folding within the intracellular environment remained a fundamental unsolved question. Franz-Ulrich Hartl contributed to the discovery that molecular chaperones, including the well-known heat shock proteins (Hsps), actively promote protein folding and prevent protein aggregation in cells—often via an energy dependent (ATP) mechanism. This groundbreaking discovery established the new paradigm that protein folding requires the assistance of molecular chaperones, an insight that fundamentally transformed the field of molecular cell biology.

F.-Ulrich Hartl also elucidated the structures and mechanisms of chaperone complexes and uncovered the cooperative chaperone network that maintains intracellular protein homeostasis. He demonstrated that a disruption in protein folding leads to toxic protein aggregation, which is a central mechanism of neurodegenerative diseases. In doing so, he laid the foundation for novel therapeutic strategies. His work has profoundly influenced both basic biomedical research and clinical medicine.

“I would like to express my sincere gratitude to the prize committee for selecting me as one of the recipients of the 2026 Keio Medical Science Prize. I am deeply honored to receive this prestigious recognition for my contributions to understanding the mechanisms of chaperone-assisted protein folding and the critical role of molecular chaperones in neurodegenerative diseases associated with protein aggregation” says Hartl. “I would like to acknowledge especially the contributions of the many talented students and postdocs I had the pleasure of working with. What began as purely curiosity-driven research ultimately yielded unexpected insights of medical relevance, hopefully leading to new therapies.”

About the Laureate

Franz-Ulrich Hartl was born in 1957. He studied Medicine at the University of Heidelberg, where he also obtained his doctoral degree. Hartl joined Walter Neupert’s research group at Ludwig Maximilians University in Munich as a postdoc and then became a group leader in Neupert’s department. A fellowship from the German Research Foundation (DFG) enabled him to undertake research at the University of California, Los Angeles. He did research as a Professor and Howard Hughes Medical Investigator at the Sloan Kettering Institute and at the Cornell University in New York, USA. In 1997, the Max Planck Society succeeded in enticing the renowned scientist back to Germany. Since then, he has been Director and head of the Department of Cellular Biochemistry at the Max Planck Institute of Biochemistry. He has received multiple scientific prizes including the Gottfried Wilhelm Leibniz Prize 2002, the Albert Lasker Award for Basic Medical Research 2011, the Shaw Prize together with Arthur L. Horwich in 2012, and 2016 the Albany Medical Center-Prize together with Horwich and Susan Lee Lindquist. In 2018, Hartl was inducted into the Hall of Fame of German Research, in 2019 he received the Dr. Paul Janssen Award and the Paul Ehrlich- and Ludwig Darmstaedter-Prize. In 2020 he was awarded the Breakthrough Prize.

About the Keio Medical Science Prize

Keio University, Japan's oldest private university, awards the Keio Medical Science Prize to honor researchers who have made outstanding contributions in the fields of medicine or the life sciences. It is the only prize of its kind awarded by a Japanese university. Thirteen recipients of this prize have subsequently been awarded the Nobel Prize. The prize is awarded annually to no more than two scientists and comes with a cash award of 10 million Japanese yen.

Glossary

Amino acids: These are the 20 basic building blocks of proteins. They are linked to form long amino acid chains, which, depending on their specific sequence, determine the structure and thus the function of a protein.

ATP (adenosine triphosphate): is a mononucleotide that has bound energy-rich phosphate residues. ATP serves as the central energy currency in biological processes.

Molecular chaperone: Member of a family of proteins that help newly produced proteins to fold