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

Molecular mechanism of membrane protein integration into the endoplasmic reticulum.
Authors: Authors: Mothes W, Heinrich SU, Graf R, Nilsson I, von Heijne G, Brunner J, Rapoport TA.
Cell
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Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction.
Authors: Authors: Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, Jones TR, Rapoport TA, Ploegh HL.
Nature
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Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation.
Authors: Authors: Hanein D, Matlack KE, Jungnickel B, Plath K, Kalies KU, Miller KR, Rapoport TA, Akey CW.
Cell
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Approaching the mechanism of protein transport across the ER membrane.
Authors: Authors: Rapoport TA, Rolls MM, Jungnickel B.
Curr Opin Cell Biol
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Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane.
Authors: Authors: Voigt S, Jungnickel B, Hartmann E, Rapoport TA.
J Cell Biol
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Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting.
Authors: Authors: Bacher G, Lütcke H, Jungnickel B, Rapoport TA, Dobberstein B.
Nature
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Synaptobrevin is essential for secretion but not for the development of synaptic processes.
Authors: Authors: Ahnert-Hilger G, Kutay U, Chahoud I, Rapoport T, Wiedenmann B.
Eur J Cell Biol
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A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae.
Authors: Authors: Finke K, Plath K, Panzner S, Prehn S, Rapoport TA, Hartmann E, Sommer T.
EMBO J
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A 12-residue-long polyleucine tail is sufficient to anchor synaptobrevin to the endoplasmic reticulum membrane.
Authors: Authors: Whitley P, Grahn E, Kutay U, Rapoport TA, von Heijne G.
J Biol Chem
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Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes.
Authors: Authors: Rapoport TA, Jungnickel B, Kutay U.
Annu Rev Biochem
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