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

A class of dynamin-like GTPases involved in the generation of the tubular ER network.
Authors: Authors: Hu J, Shibata Y, Zhu PP, Voss C, Rismanchi N, Prinz WA, Rapoport TA, Blackstone C.
Cell
View full abstract on Pubmed
Mechanisms shaping the membranes of cellular organelles.
Authors: Authors: Shibata Y, Hu J, Kozlov MM, Rapoport TA.
Annu Rev Cell Dev Biol
View full abstract on Pubmed
A role for the two-helix finger of the SecA ATPase in protein translocation.
Authors: Authors: Erlandson KJ, Miller SB, Nam Y, Osborne AR, Zimmer J, Rapoport TA.
Nature
View full abstract on Pubmed
Structure of a complex of the ATPase SecA and the protein-translocation channel.
Authors: Authors: Zimmer J, Nam Y, Rapoport TA.
Nature
View full abstract on Pubmed
Protein transport across the endoplasmic reticulum membrane.
Authors: Authors: Rapoport TA.
FEBS J
View full abstract on Pubmed
The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum.
Authors: Authors: Shibata Y, Voss C, Rist JM, Hu J, Rapoport TA, Prinz WA, Voeltz GK.
J Biol Chem
View full abstract on Pubmed
Single copies of Sec61 and TRAP associate with a nontranslating mammalian ribosome.
Authors: Authors: Ménétret JF, Hegde RS, Aguiar M, Gygi SP, Park E, Rapoport TA, Akey CW.
Structure
View full abstract on Pubmed
Analysis of polypeptide movement in the SecY channel during SecA-mediated protein translocation.
Authors: Authors: Erlandson KJ, Or E, Osborne AR, Rapoport TA.
J Biol Chem
View full abstract on Pubmed
The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p.
Authors: Authors: Goder V, Carvalho P, Rapoport TA.
FEBS Lett
View full abstract on Pubmed
Membrane proteins of the endoplasmic reticulum induce high-curvature tubules.
Authors: Authors: Hu J, Shibata Y, Voss C, Shemesh T, Li Z, Coughlin M, Kozlov MM, Rapoport TA, Prinz WA.
Science
View full abstract on Pubmed