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

Unique double-ring structure of the peroxisomal Pex1/Pex6 ATPase complex revealed by cryo-electron microscopy.
Authors: Authors: Blok NB, Tan D, Wang RY, Penczek PA, Baker D, DiMaio F, Rapoport TA, Walz T.
Proc Natl Acad Sci U S A
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Conformational Changes of the Clamp of the Protein Translocation ATPase SecA.
Authors: Authors: Chen Y, Bauer BW, Rapoport TA, Gumbart JC.
J Mol Biol
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Cis and trans interactions between atlastin molecules during membrane fusion.
Authors: Authors: Liu TY, Bian X, Romano FB, Shemesh T, Rapoport TA, Hu J.
Proc Natl Acad Sci U S A
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Decatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon.
Authors: Authors: Junne T, Wong J, Studer C, Aust T, Bauer BW, Beibel M, Bhullar B, Bruccoleri R, Eichenberger J, Estoppey D, Hartmann N, Knapp B, Krastel P, Melin N, Oakeley EJ, Oberer L, Riedl R, Roma G, Schuierer S, Petersen F, Tallarico JA, Rapoport TA, Spiess M, Hoepfner D.
J Cell Sci
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A model for the generation and interconversion of ER morphologies.
Authors: Authors: Shemesh T, Klemm RW, Romano FB, Wang S, Vaughan J, Zhuang X, Tukachinsky H, Kozlov MM, Rapoport TA.
Proc Natl Acad Sci U S A
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Key steps in ERAD of luminal ER proteins reconstituted with purified components.
Authors: Authors: Stein A, Ruggiano A, Carvalho P, Rapoport TA.
Cell
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A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPase.
Authors: Authors: Bauer BW, Shemesh T, Chen Y, Rapoport TA.
Cell
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Structure of the SecY channel during initiation of protein translocation.
Authors: Authors: Park E, Ménétret JF, Gumbart JC, Ludtke SJ, Li W, Whynot A, Rapoport TA, Akey CW.
Nature
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Structural analysis and optimization of the covalent association between SpyCatcher and a peptide Tag.
Authors: Authors: Li L, Fierer JO, Rapoport TA, Howarth M.
J Mol Biol
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An ER protein functionally couples neutral lipid metabolism on lipid droplets to membrane lipid synthesis in the ER.
Authors: Authors: Markgraf DF, Klemm RW, Junker M, Hannibal-Bach HK, Ejsing CS, Rapoport TA.
Cell Rep
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