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

Light chain-dependent regulation of Kinesin's interaction with microtubules.
Authors: Authors: Verhey KJ, Lizotte DL, Abramson T, Barenboim L, Schnapp BJ, Rapoport TA.
J Cell Biol
View full abstract on Pubmed
J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences.
Authors: Authors: Misselwitz B, Staeck O, Rapoport TA.
Mol Cell
View full abstract on Pubmed
Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.
Authors: Authors: Plath K, Mothes W, Wilkinson BM, Stirling CJ, Rapoport TA.
Cell
View full abstract on Pubmed
Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane.
Authors: Authors: Mothes W, Jungnickel B, Brunner J, Rapoport TA.
J Cell Biol
View full abstract on Pubmed
The beta subunit of the Sec61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation.
Authors: Authors: Kalies KU, Rapoport TA, Hartmann E.
J Cell Biol
View full abstract on Pubmed
TRAM regulates the exposure of nascent secretory proteins to the cytosol during translocation into the endoplasmic reticulum.
Authors: Authors: Hegde RS, Voigt S, Rapoport TA, Lingappa VR.
Cell
View full abstract on Pubmed
Protein translocation: tunnel vision.
Authors: Authors: Matlack KE, Mothes W, Rapoport TA.
Cell
View full abstract on Pubmed
Binding of signal recognition particle gives ribosome/nascent chain complexes a competitive advantage in endoplasmic reticulum membrane interaction.
Authors: Authors: Neuhof A, Rolls MM, Jungnickel B, Kalies KU, Rapoport TA.
Mol Biol Cell
View full abstract on Pubmed
Women in black: challenging Israel's gender and socio-political orders.
Authors: Authors: Helman S, Rapoport T.
Br J Sociol
View full abstract on Pubmed
Protein transport by purified yeast Sec complex and Kar2p without membranes.
Authors: Authors: Matlack KE, Plath K, Misselwitz B, Rapoport TA.
Science
View full abstract on Pubmed