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

Protein transport across the ER membrane.
Authors: Authors: Rapoport TA.
Trends Biochem Sci
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Structure and biosynthesis of the signal-sequence receptor.
Authors: Authors: Prehn S, Herz J, Hartmann E, Kurzchalia TV, Frank R, Roemisch K, Dobberstein B, Rapoport TA.
Eur J Biochem
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A novel pathway for secretory proteins?
Authors: Authors: Muesch A, Hartmann E, Rohde K, Rubartelli A, Sitia R, Rapoport TA.
Trends Biochem Sci
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Developmental assumptions in literary criticism and their implications for conceptions of continuity and change in literary creativity.
Authors: Authors: Cohen-Shalev A, Rapoport T.
Psychol Aging
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Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum.
Authors: Authors: Wiedmann M, Goerlich D, Hartmann E, Kurzchalia TV, Rapoport TA.
FEBS Lett
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Cytosolic protein translocation factors. Is SRP still unique?
Authors: Authors: Bernstein HD, Rapoport TA, Walter P.
Cell
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A membrane component of the endoplasmic reticulum that may be essential for protein translocation.
Authors: Authors: Hartmann E, Wiedmann M, Rapoport TA.
EMBO J
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Predicting the orientation of eukaryotic membrane-spanning proteins.
Authors: Authors: Hartmann E, Rapoport TA, Lodish HF.
Proc Natl Acad Sci U S A
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Complex role experiences and personal differentiation: a real-life experiment.
Authors: Authors: Rapoport T, Rosenhek Z.
J Adolesc
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Signal recognition in protein translocation across the endoplasmic reticulum membrane.
Authors: Authors: Rapoport TA, Wiedmann M, Kurzchalia TV, Hartmann E.
Biochem Soc Trans
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