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| Name |
Rapoport, Tom A. |
| Location
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Harvard Medical School |
| Primary Field
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Biochemistry |
| Secondary Field
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Cellular and Developmental Biology |
 Election Citation
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Rapoport identified and characterized countless components of the protein translocation apparatus of the mammalian endoplasmic reticulum membrane, revealing how this molecular loading dock operates. He demonstrated co- and post-translational transport with reconstituted proteoliposomes and revolutionized the field of cell biology by determining the structure of the protein-conducting channel. |
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Research Interests
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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. |
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