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

Interactions between Sec complex and prepro-alpha-factor during posttranslational protein transport into the endoplasmic reticulum.
Authors: Authors: Plath K, Wilkinson BM, Stirling CJ, Rapoport TA.
Mol Biol Cell
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Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm.
Authors: Authors: Fujinaga Y, Wolf AA, Rodighiero C, Wheeler H, Tsai B, Allen L, Jobling MG, Rapoport T, Holmes RK, Lencer WI.
Mol Biol Cell
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Polyubiquitin serves as a recognition signal, rather than a ratcheting molecule, during retrotranslocation of proteins across the endoplasmic reticulum membrane.
Authors: Authors: Flierman D, Ye Y, Dai M, Chau V, Rapoport TA.
J Biol Chem
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Gangliosides are receptors for murine polyoma virus and SV40.
Authors: Authors: Tsai B, Gilbert JM, Stehle T, Lencer W, Benjamin TL, Rapoport TA.
EMBO J
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Cooperation of transmembrane segments during the integration of a double-spanning protein into the ER membrane.
Authors: Authors: Heinrich SU, Rapoport TA.
EMBO J
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Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains.
Authors: Authors: Ye Y, Meyer HH, Rapoport TA.
J Cell Biol
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Structure of the mammalian ribosome-channel complex at 17A resolution.
Authors: Authors: Morgan DG, Ménétret JF, Neuhof A, Rapoport TA, Akey CW.
J Mol Biol
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Role of ubiquitination in retro-translocation of cholera toxin and escape of cytosolic degradation.
Authors: Authors: Rodighiero C, Tsai B, Rapoport TA, Lencer WI.
EMBO Rep
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Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1.
Authors: Authors: Tsai B, Rapoport TA.
J Cell Biol
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Structural organization of the endoplasmic reticulum.
Authors: Authors: Voeltz GK, Rolls MM, Rapoport TA.
EMBO Rep
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