Tom Rapoport
Tom Rapoport, Ph.D.
Professor of Cell Biology (HMS)
HHMI Investigator

Tom Rapoport, Ph.D., joined the faculty at Harvard Medical School in 1995. He received his Ph.D. in Biochemistry from the Humboldt University in East-Berlin for work in enzymology. He then focused on mathematical modeling of metabolism, for which he received his second degree (Habilitation) from the same institution. Before moving to the US, he worked at the Central Institute of Molecular Biology of the Academy of Sciences of the GDR and later at the Max-Delbrueck Center for Molecular Medicine in Berlin-Buch. In 1997, he became a Howard Hughes Medical Institute Investigator.

The Rapoport Lab is interested in the mechanisms by which proteins are transported across membranes, how misfolded proteins are degraded, and how organelles form and maintain their characteristic shapes. Most of the projects center around the endoplasmic reticulum (ER). One project concerns the molecular mechanism by which proteins are translocated across the ER membrane or across the plasma membrane in bacteria and archaea. Much of the current work deals with ERAD (ER-associated protein degradation), a process in which misfolded proteins are retro-translocated across the ER membrane into the cytosol. Major questions concern the mechanism by which proteins move across the membrane and are extracted by the Cdc48 ATPase. Another project concerns the mechanism by which ER morphology, specifically the tubular ER network, is generated. More recently, the Rapoport lab has started to study how proteins are imported into peroxisomes, and how lung surfactant proteins generate lamellar bodies. The lab employs a variety of different techniques, including biochemical methods, such as reconstitutions with purified proteins, and structural biology methods, including X-ray crystallography and cryo-electron microscopy.

Harvard Medical School

Dept. of Cell Biology, LHRRB 401

240 Longwood Avenue

Boston, MA 02115

Lab phone: 617-432-1612

Lab fax: 617-432-1190

Translocation of polyubiquitinated protein substrates by the hexameric Cdc48 ATPase.
Authors: Authors: Ji Z, Li H, Peterle D, Paulo JA, Ficarro SB, Wales TE, Marto JA, Gygi SP, Engen JR, Rapoport TA.
Mol Cell
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Cryo-EM structure determination of small proteins by nanobody-binding scaffolds (Legobodies).
Authors: Authors: Wu X, Rapoport TA.
Proc Natl Acad Sci U S A
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Translocation of Proteins through a Distorted Lipid Bilayer.
Authors: Authors: Wu X, Rapoport TA.
Trends Cell Biol
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Mechanism of membrane-curvature generation by ER-tubule shaping proteins.
Authors: Authors: Wang N, Clark LD, Gao Y, Kozlov MM, Shemesh T, Rapoport TA.
Nat Commun
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Mechanism of Lamellar Body Formation by Lung Surfactant Protein B.
Authors: Authors: Sever N, Milicic G, Bodnar NO, Wu X, Rapoport TA.
Mol Cell
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Protease protection assays show polypeptide movement into the SecY channel by power strokes of the SecA ATPase.
Authors: Authors: Catipovic MA, Rapoport TA.
EMBO Rep
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Structural basis of ER-associated protein degradation mediated by the Hrd1 ubiquitin ligase complex.
Authors: Authors: Wu X, Siggel M, Ovchinnikov S, Mi W, Svetlov V, Nudler E, Liao M, Hummer G, Rapoport TA.
Science
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Ddi1 is a ubiquitin-dependent protease.
Authors: Authors: Yip MCJ, Bodnar NO, Rapoport TA.
Proc Natl Acad Sci U S A
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Cycles of autoubiquitination and deubiquitination regulate the ERAD ubiquitin ligase Hrd1.
Authors: Authors: Peterson BG, Glaser ML, Rapoport TA, Baldridge RD.
Elife
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Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding.
Authors: Authors: Twomey EC, Ji Z, Wales TE, Bodnar NO, Ficarro SB, Marto JA, Engen JR, Rapoport TA.
Science
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