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

Signal sequence processing in rough microsomes.
Authors: Authors: Lyko F, Martoglio B, Jungnickel B, Rapoport TA, Dobberstein B.
J Biol Chem
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A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane.
Authors: Authors: Jungnickel B, Rapoport TA.
Cell
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Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p.
Authors: Authors: Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport TA.
Cell
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The Sec61 complex is essential for the insertion of proteins into the membrane of the endoplasmic reticulum.
Authors: Authors: Oliver J, Jungnickel B, Görlich D, Rapoport T, High S.
FEBS Lett
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Transport route for synaptobrevin via a novel pathway of insertion into the endoplasmic reticulum membrane.
Authors: Authors: Kutay U, Ahnert-Hilger G, Hartmann E, Wiedenmann B, Rapoport TA.
EMBO J
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Posttranslational protein transport into the endoplasmic reticulum.
Authors: Authors: Panzner S, Dreier L, Hartmann E, Kostka S, Rapoport TA.
Cold Spring Harb Symp Quant Biol
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Systematic probing of the environment of a translocating secretory protein during translocation through the ER membrane.
Authors: Authors: Mothes W, Prehn S, Rapoport TA.
EMBO J
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Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex.
Authors: Authors: Kalies KU, Görlich D, Rapoport TA.
J Cell Biol
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Protein translocation: common themes from bacteria to man.
Authors: Authors: Jungnickel B, Rapoport TA, Hartmann E.
FEBS Lett
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Evolutionary conservation of components of the protein translocation complex.
Authors: Authors: Hartmann E, Sommer T, Prehn S, Görlich D, Jentsch S, Rapoport TA.
Nature
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