Tom Rapoport

Tom Rapoport, Ph.D.

Don W. Fawcett Professor of Cell Biology (HMS)
HHMI Investigator
LHRRB 401

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

Recognition of an ERAD-L substrate analyzed by site-specific in vivo photocrosslinking.
Authors: Authors: Stanley AM, Carvalho P, Rapoport T.
FEBS Lett
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Structures of the atlastin GTPase provide insight into homotypic fusion of endoplasmic reticulum membranes.
Authors: Authors: Bian X, Klemm RW, Liu TY, Zhang M, Sun S, Sui X, Liu X, Rapoport TA, Hu J.
Proc Natl Acad Sci U S A
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Processing and turnover of the Hedgehog protein in the endoplasmic reticulum.
Authors: Authors: Chen X, Tukachinsky H, Huang CH, Jao C, Chu YR, Tang HY, Mueller B, Schulman S, Rapoport TA, Salic A.
J Cell Biol
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Mechanisms determining the morphology of the peripheral ER.
Authors: Authors: Shibata Y, Shemesh T, Prinz WA, Palazzo AF, Kozlov MM, Rapoport TA.
Cell
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A preliminary report on my life in science.
Authors: Authors: Rapoport TA.
Mol Biol Cell
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Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p.
Authors: Authors: Carvalho P, Stanley AM, Rapoport TA.
Cell
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Vitamin K epoxide reductase prefers ER membrane-anchored thioredoxin-like redox partners.
Authors: Authors: Schulman S, Wang B, Li W, Rapoport TA.
Proc Natl Acad Sci U S A
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Structure of a bacterial homologue of vitamin K epoxide reductase.
Authors: Authors: Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA.
Nature
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Conformational flexibility and peptide interaction of the translocation ATPase SecA.
Authors: Authors: Zimmer J, Rapoport TA.
J Mol Biol
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Mapping polypeptide interactions of the SecA ATPase during translocation.
Authors: Authors: Bauer BW, Rapoport TA.
Proc Natl Acad Sci U S A
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