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

Internally transposed signal sequence of carp preproinsulin retains its functions with the signal recognition particle.
Authors: Authors: Wiedmann M, Huth A, Rapoport TA.
FEBS Lett
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Protein translocation across and integration into membranes.
Authors: Authors: Rapoport TA.
CRC Crit Rev Biochem
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Extensions of the signal hypothesis--sequential insertion model versus amphipathic tunnel hypothesis.
Authors: Authors: Rapoport TA.
FEBS Lett
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Molecular cloning and identification of cDNA recombinants coding for bovine prochymosin in E. coli.
Authors: Authors: Liebscher DH, Lipoldová M, Smrt J, Schwertner S, Wambutt R, Speter W, Pöhlmann C, Pfeifer M, Hahn V, Rapoport TA, et al.
Folia Biol (Praha)
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Application of the signal hypothesis to the incorporation of integral membrane proteins
Authors: Authors: Rapoport TA, Wiedmann M
Curr Top Mem Trans
Xenopus oocytes can secrete bacterial beta-lactamase.
Authors: Authors: Wiedmann M, Huth A, Rapoport TA.
Nature
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Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface.
Authors: Authors: Huth A, Rapoport TA, Kääriäinen L.
EMBO J
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Signal recognition particle triggers the translocation of storage globulin polypeptides from field beans (Vicia faba L.) across mammalian endoplasmic reticulum membrane.
Authors: Authors: Bassüner R, Wobus U, Rapoport TA.
FEBS Lett
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Carp preproinsulin cDNA sequence and evolution of insulin genes.
Authors: Authors: Hahn V, Winkler J, Rapoport TA, Liebscher DH, Coutelle C, Rosenthal S.
Folia Biol (Praha)
View full abstract on Pubmed
Expression of the DNA sequence coding for carp preproinsulin in E.coli-initiation of translation at the eukaryotic start condon
Authors: Authors: Pfeiffer M, Hahn V, Huth A, Liebscher DH, Pöhlmann CH, Rapoport TA, Rosenthal S, Tran-Batcke A, Wolf M
Biol Zbl