Tom Rapoport

Tom Rapoport, Ph.D.

Don W. Fawcett 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

Mechanistic insights into ER-associated protein degradation.
Authors: Authors: Wu X, Rapoport TA.
Curr Opin Cell Biol
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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
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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
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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
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Structural and Mechanistic Insights into Protein Translocation.
Authors: Authors: Rapoport TA, Li L, Park E.
Annu Rev Cell Dev Biol
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Cryo-EM structure of the protein-conducting ERAD channel Hrd1 in complex with Hrd3.
Authors: Authors: Schoebel S, Mi W, Stein A, Ovchinnikov S, Pavlovicz R, DiMaio F, Baker D, Chambers MG, Su H, Li D, Rapoport TA, Liao M.
Nature
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Two alternative binding mechanisms connect the protein translocation Sec71-Sec72 complex with heat shock proteins.
Authors: Authors: Tripathi A, Mandon EC, Gilmore R, Rapoport TA.
J Biol Chem
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Molecular Mechanism of Substrate Processing by the Cdc48 ATPase Complex.
Authors: Authors: Bodnar NO, Rapoport TA.
Cell
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Reconstitution of the tubular endoplasmic reticulum network with purified components.
Authors: Authors: Powers RE, Wang S, Liu TY, Rapoport TA.
Nature
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Toward an understanding of the Cdc48/p97 ATPase.
Authors: Authors: Bodnar N, Rapoport T.
F1000Res
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