Tom A. Rapoport

Harvard University


Primary Section: 21, Biochemistry
Secondary Section: 22, Cellular and Developmental Biology
Membership Type:
Member (elected 2005)

Biosketch

Dr. Tom Rapoport is a Professor of Cell Biology at Harvard Medical School and a Howard Hughes Medical School investigator. He is a biochemist and cell biologist. Rapoport is known for the development of the Metabolic Control Analysis (MCA) (together with Reinhart Heinrich), for the elucidation of mechanisms by which proteins are translocated across the eukaryotic  endoplasmic reticulum (ER) membrane and the bacterial plasma membrane, for the first structure of a protein-conducting channel (together with Steve Harrison), for the elucidation of the mechanism of ER-associated protein degradation (ERAD), and the identification of components and mechanisms that generate the characteristic shape of the ER.  Dr. Rapoport earned his Ph.D. from Humboldt University (Berlin; East Germany) in 1972. He then worked at the Zentralinstitut für Molekularbiologie der Akademie der Wissenschaften der DDR in Berlin, which later became the Max-Delbrück-Institute. In 1995, he joined the faculty of Harvard Medical School, and in 1997, he became a Howard Hughes Medical Institute Investigator. Rapoport is a member of the National Academies of the USA and Germany.  He has received several awards.

Research Interests

Tom Rapoport's laboratory is interested in the molecular mechanism by which proteins are transported across membranes and by which organelles are shaped. His group has used biochemical and structural methods to elucidate the mechanism of protein translocation. They reconstituted protein translocation into the ER with purified components, identified the Sec61 complex as the protein-conducting channel, determined the first structure of a protein-conducting channel (together with Steve Harrison), and clarified the molecular mechanism of different modes of translocation. Another area of research concerns ERAD. Major discoveries include the identification of the essential role of the p97 (Cdc48) ATPase, the reconstitution of a basic ERAD process with purified components, the elucidation of the mechanism of the Cdc48 ATPase, and the structure of the retro-translocon. Rapoport has also started a field that is directed towards an understanding of how organelles are shaped. His lab has identified proteins that form ER tubules, fusion GTPases that connect the tubules into a network, and has reconstituted ER network formation with purified proteins. His lab also studies protein import into peroxisomes and the generation of lung surfactant.

Powered by Blackbaud
nonprofit software