Ulrich Hartl studied Medicine at Heidelberg University and received a doctoral degree in Biochemistry in 1985. He then worked with Walter Neupert in Munich on protein import into mitochondria. In 1987, Hartl began studies on molecular chaperones and demonstrated, together with Arthur Horwich, the basic role of chaperones in assisting protein folding. After a stay with William Wickner at UCLA (1989/1990), Hartl returned to Munich to receive his Habilitation in Biochemistry. He then accepted an offer from Sloan-Kettering Cancer Center in New York to join the department of James Rothman as an Associate Member. Between 1991 and 1997 Hartl, in collaboration with Manajit Hayer-Hartl, worked on protein folding in the bacterial and eukaryotic cytosol. They reconstituted the pathway of chaperone-assisted folding in which the Hsp70 and the GroEL chaperone systems cooperate and discovered that GroEL and its co-factor GroES provide a cage for individual protein molecules to fold unimpaired by aggregation. In 1993 Hartl was promoted to Member with tenure, and in 1994 became HHMI Investigator. In 1997, he returned to Munich to head the Department of Cellular Biochemistry at Max Planck Institute of Biochemistry. At MPIB Hartl initiated research into neurodegenerative diseases caused by protein misfolding and aggregation.

Research Interests

Research in the Hartl laboratory focuses on the mechanisms of protein folding and quality control in the cell. Our goal is to reach a comprehensive understanding, at the structural and functional level, of how the machinery of molecular chaperones assists folding through the cooperation of co- and post-translational mechanisms. A long-standing interest is to understand how the cylindrical chaperonins of the GroEL type promote and modulate the folding process. Our second major research focus concerns the molecular mechanisms of proteotoxicity in diseases associated with protein misfolding and aggregation, including Parkinson's, Alzheimer's and Huntington's diseases. Here we wish to understand how the cellular machinery of protein homeostasis (proteostasis) normally provides protection and why these defense mechanisms increasingly fail during aging, facilitating the manifestation of neurodegeneration. We are using a wide range of methods from cellular biochemistry, biophysics and structural biology. In understanding the proteostasis network we are increasingly using systems-based approaches, including quantitative proteomics and genetic screens.

Membership Type

International Member

Election Year


Primary Section

Section 21: Biochemistry