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

Polyubiquitination is required for US11-dependent movement of MHC class I heavy chain from endoplasmic reticulum into cytosol.
Authors: Authors: Shamu CE, Flierman D, Ploegh HL, Rapoport TA, Chau V.
Mol Biol Cell
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Projection structure and oligomeric properties of a bacterial core protein translocase.
Authors: Authors: Collinson I, Breyton C, Duong F, Tziatzios C, Schubert D, Or E, Rapoport T, Kühlbrandt W.
EMBO J
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Protein disulfide isomerase acts as a redox-dependent chaperone to unfold cholera toxin.
Authors: Authors: Tsai B, Rodighiero C, Lencer WI, Rapoport TA.
Cell
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Cargo of kinesin identified as JIP scaffolding proteins and associated signaling molecules.
Authors: Authors: Verhey KJ, Meyer D, Deehan R, Blenis J, Schnapp BJ, Rapoport TA, Margolis B.
J Cell Biol
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Ratcheting in post-translational protein translocation: a mathematical model.
Authors: Authors: Liebermeister W, Rapoport TA, Heinrich R.
J Mol Biol
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The structure of ribosome-channel complexes engaged in protein translocation.
Authors: Authors: Menetret JF, Neuhof A, Morgan DG, Plath K, Radermacher M, Rapoport TA, Akey CW.
Mol Cell
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Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum.
Authors: Authors: Plath K, Rapoport TA.
J Cell Biol
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A comparison of the yeast and rabbit 80 S ribosome reveals the topology of the nascent chain exit tunnel, inter-subunit bridges and mammalian rRNA expansion segments.
Authors: Authors: Morgan DG, Ménétret JF, Radermacher M, Neuhof A, Akey IV, Rapoport TA, Akey CW.
J Mol Biol
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Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae.
Authors: Authors: Prinz WA, Grzyb L, Veenhuis M, Kahana JA, Silver PA, Rapoport TA.
J Cell Biol
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The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain.
Authors: Authors: Heinrich SU, Mothes W, Brunner J, Rapoport TA.
Cell
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