Albert Lasker
Basic Medical Research Award

Acceptance Remarks by Franz-Ulrich Hartl

Receiving the Lasker Basic Medical Research Award is a tremendous honor and a great privilege. I am pleased to receive this award together with Art Horwich with whom I share exciting memories of the early phase of discovery in the molecular chaperone field. I am very grateful to the Lasker Foundation and especially to the Lasker Jury for selecting us, and I wish to express my gratitude to the many people who have supported and "chaperoned" me along the way, especially my wife and long-term collaborator Manajit.

To be recognized by a Lasker award is of course the dream of every biochemist or molecular biologist. I am amazed that this dream has become a reality for me. But we should not forget that our true reward as scientists is the privilege of doing something that we enjoy so deeply and that doesn't feel like work at all. I am well aware that our discoveries were only possible because many others who came before us laid the foundation. This, and a large quantity of good fortune, allowed us to make the surprising finding, in the late 1980s, that proteins, the molecules that drive almost every biological process, reach their proper shape (their "fold") by the help of other proteins, which we call molecular chaperones. This was unexpected in light of the widely held view at the time that protein folding occurs spontaneously. It was my mentor Walter Neupert at Munich University who introduced me to Art. Walter supported us with his insight and provided the environment in which our collaboration could be successful. The mechanisms we eventually uncovered are beautiful in their simplicity: A large barrel-shaped protein complex, called chaperonin, functions like a mini-test tube in the cell, allowing immature protein molecules to fold, one at a time, while being shielded from the densely populated cellular milieu. As a result, new protein chains are protected from clumping together — just like the human chaperone prevents improper interactions between young people.

I grew up in a small village in the northern part of the Black Forest. Early on in high school I developed a strong interest in biology and chemistry. In my second year of Medical School at Heidelberg University I was given the chance to work in the biochemistry lab. I quickly realized that this was what I wanted to do, rather than practicing medicine. Who knows how many lives I saved by that decision. In any case, I was hooked by research, despite the frustrations when experiments didn't work. I remember vividly the Hungarian guest researcher who spent hours and hours in the cold room isolating proteins. When he emerged, apparently quite exhausted, he would invariably say "Biochemie ist kein Spaziergang" ("Biochemistry is not a walk in the park."). Owing to many fortunate circumstances, I can say that for me biochemistry became the path to a very exciting and rewarding life.

In recent years research in a number of laboratories provided evidence for the medical relevance of molecular chaperones in preventing the formation of protein aggregates that cause presently incurable diseases like Alzheimer's, Parkinson's or Huntington's disease. Hopefully, one day it will be possible to harness the power of molecular chaperones for the treatment of these diseases. Should this happen, I can honestly say it was not planned, since for the most part I just wanted to find out a bit more about the fascinating workings of cells, without any application in mind. Unfortunately, science policy makers often do not realize the potential benefits of supporting such basic research. It is to the credit of organizations like the Lasker Foundation that the public is made aware of how scientific progress is most often achieved, namely through pure curiosity driven research.

Finally, let me say what a great pleasure and honor it is to receive this award here in New York, the city in which my wife and I have spent some of the best years of our life and where we have so many wonderful friends.