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

Multiple mechanisms determine ER network morphology during the cell cycle in Xenopus egg extracts.
Authors: Authors: Wang S, Romano FB, Field CM, Mitchison TJ, Rapoport TA.
J Cell Biol
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Stacked endoplasmic reticulum sheets are connected by helicoidal membrane motifs.
Authors: Authors: Terasaki M, Shemesh T, Kasthuri N, Klemm RW, Schalek R, Hayworth KJ, Hand AR, Yankova M, Huber G, Lichtman JW, Rapoport TA, Kozlov MM.
Cell
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A conserved role for atlastin GTPases in regulating lipid droplet size.
Authors: Authors: Klemm RW, Norton JP, Cole RA, Li CS, Park SH, Crane MM, Li L, Jin D, Boye-Doe A, Liu TY, Shibata Y, Lu H, Rapoport TA, Farese RV, Blackstone C, Guo Y, Mak HY.
Cell Rep
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Bacterial protein translocation requires only one copy of the SecY complex in vivo.
Authors: Authors: Park E, Rapoport TA.
J Cell Biol
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Lipid interaction of the C terminus and association of the transmembrane segments facilitate atlastin-mediated homotypic endoplasmic reticulum fusion.
Authors: Authors: Liu TY, Bian X, Sun S, Hu X, Klemm RW, Prinz WA, Rapoport TA, Hu J.
Proc Natl Acad Sci U S A
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Gem1 and ERMES do not directly affect phosphatidylserine transport from ER to mitochondria or mitochondrial inheritance.
Authors: Authors: Nguyen TT, Lewandowska A, Choi JY, Markgraf DF, Junker M, Bilgin M, Ejsing CS, Voelker DR, Rapoport TA, Shaw JM.
Traffic
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The dynamin-like GTPase Sey1p mediates homotypic ER fusion in S. cerevisiae.
Authors: Authors: Anwar K, Klemm RW, Condon A, Severin KN, Zhang M, Ghirlando R, Hu J, Rapoport TA, Prinz WA.
J Cell Biol
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Mechanisms of Sec61/SecY-mediated protein translocation across membranes.
Authors: Authors: Park E, Rapoport TA.
Annu Rev Biophys
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Weaving the web of ER tubules.
Authors: Authors: Hu J, Prinz WA, Rapoport TA.
Cell
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Preserving the membrane barrier for small molecules during bacterial protein translocation.
Authors: Authors: Park E, Rapoport TA.
Nature
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