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

Recognition of signal sequences.
Authors: Authors: Finkelstein AV, Bendzko P, 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.
Nucleic Acids Res
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Secretion of plant storage globulin polypeptides by Xenopus laevis oocytes.
Authors: Authors: Bassüner R, Huth A, Manteuffel R, Rapoport TA.
Eur J Biochem
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Transport of proteins and signal recognition
Authors: Authors: Rapoport TA, Huth A, Proesch S, Bendzko P, Kaeaeriaeinen L, Bassuner R, Manteuffel R, Finkelstein A
Protein synthesis (Abraham AKK, Eikhom TS, Pryme IF)
Carp preproinsulin cDNA sequence and evolution of insulin genes
Authors: Authors: Hahn V, Winkler J, Rapoport TA, Liebscher DH, Coutelle CH, Rosenthal S
Nucl Acid Res
Different modes of membrane interactions of the signal sequence of carp preproinsulin and of the insertion sequence of rabbit cytochrome b5.
Authors: Authors: Bendzko P, Prehn S, Pfeil W, Rapoport TA.
Eur J Biochem
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Regulation of the biosynthesis of insulin in isolated Brockmann bodies of the carp (Cyprinus carpio).
Authors: Authors: Huth A, Rapoport TA.
Gen Comp Endocrinol
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Carp insulin: amino acid sequence, biological activity and structural properties.
Authors: Authors: Makower A, Dettmer R, Rapoport TA, Knospe S, Behlke J, Prehn S, Franke P, Etzold G, Rosenthal S.
Eur J Biochem
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Intracellular compartmentation and secretion of carp proinsulin synthesized in Xenopus oocytes.
Authors: Authors: Rapoport TA.
Eur J Biochem
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A receptor for single segments of secretory proteins in rough endoplasmic reticulum membranes.
Authors: Authors: Prehn S, Nürnberg P, Rapoport TA.
FEBS Lett
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