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

Ribosome binding to and dissociation from translocation sites of the endoplasmic reticulum membrane.
Authors: Authors: Schaletzky J, Rapoport TA.
Mol Biol Cell
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Rough sheets and smooth tubules.
Authors: Authors: Shibata Y, Voeltz GK, Rapoport TA.
Cell
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E2-25K mediates US11-triggered retro-translocation of MHC class I heavy chains in a permeabilized cell system.
Authors: Authors: Flierman D, Coleman CS, Pickart CM, Rapoport TA, Chau V.
Proc Natl Acad Sci U S A
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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins.
Authors: Authors: Carvalho P, Goder V, Rapoport TA.
Cell
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A class of membrane proteins shaping the tubular endoplasmic reticulum.
Authors: Authors: Voeltz GK, Prinz WA, Shibata Y, Rist JM, Rapoport TA.
Cell
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Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane.
Authors: Authors: Ye Y, Shibata Y, Kikkert M, van Voorden S, Wiertz E, Rapoport TA.
Proc Natl Acad Sci U S A
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Role of p97 AAA-ATPase in the retrotranslocation of the cholera toxin A1 chain, a non-ubiquitinated substrate.
Authors: Authors: Kothe M, Ye Y, Wagner JS, De Luca HE, Kern E, Rapoport TA, Lencer WI.
J Biol Chem
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Architecture of the ribosome-channel complex derived from native membranes.
Authors: Authors: Ménétret JF, Hegde RS, Heinrich SU, Chandramouli P, Ludtke SJ, Rapoport TA, Akey CW.
J Mol Biol
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Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY.
Authors: Authors: Cannon KS, Or E, Clemons WM, Shibata Y, Rapoport TA.
J Cell Biol
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The bacterial ATPase SecA functions as a monomer in protein translocation.
Authors: Authors: Or E, Boyd D, Gon S, Beckwith J, Rapoport T.
J Biol Chem
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