Tom Rapoport

Tom Rapoport, Ph.D.

Professor of Cell Biology (HMS)
HHMI Investigator

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

Lab fax: 617-432-1190

Structure of the substrate-engaged SecA-SecY protein translocation machine.
Authors: Authors: Ma C, Wu X, Sun D, Park E, Catipovic MA, Rapoport TA, Gao N, Li L.
Nat Commun
View full abstract on Pubmed
Peroxisome protein import recapitulated in Xenopus egg extracts.
Authors: Authors: Romano FB, Blok NB, Rapoport TA.
J Cell Biol
View full abstract on Pubmed
Protein translocation by the SecA ATPase occurs by a power-stroke mechanism.
Authors: Authors: Catipovic MA, Bauer BW, Loparo JJ, Rapoport TA.
EMBO J
View full abstract on Pubmed
Endoplasmic Reticulum Network Formation with Xenopus Egg Extracts.
Authors: Authors: Wang S, Romano FB, Rapoport TA.
Cold Spring Harb Protoc
View full abstract on Pubmed
Structure of the post-translational protein translocation machinery of the ER membrane.
Authors: Authors: Wu X, Cabanos C, Rapoport TA.
Nature
View full abstract on Pubmed
Reconstituting the reticular ER network - mechanistic implications and open questions.
Authors: Authors: Wang N, Rapoport TA.
J Cell Sci
View full abstract on Pubmed
Mechanistic insights into ER-associated protein degradation.
Authors: Authors: Wu X, Rapoport TA.
Curr Opin Cell Biol
View full abstract on Pubmed
Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4.
Authors: Authors: Bodnar NO, Kim KH, Ji Z, Wales TE, Svetlov V, Nudler E, Engen JR, Walz T, Rapoport TA.
Nat Struct Mol Biol
View full abstract on Pubmed
Unraveling the sequence of cytosolic reactions in the export of GspB adhesin from Streptococcus gordonii.
Authors: Authors: Chen Y, Bensing BA, Seepersaud R, Mi W, Liao M, Jeffrey PD, Shajahan A, Sonon RN, Azadi P, Sullam PM, Rapoport TA.
J Biol Chem
View full abstract on Pubmed
The ER morphology-regulating lunapark protein induces the formation of stacked bilayer discs.
Authors: Authors: Wang S, Powers RE, Gold VA, Rapoport TA.
Life Sci Alliance
View full abstract on Pubmed