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

Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA.
Authors: Authors: Prinz A, Behrens C, Rapoport TA, Hartmann E, Kalies KU.
EMBO J
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In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction.
Authors: Authors: Dreier L, Rapoport TA.
J Cell Biol
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Ran is associated with chromosomes during starfish oocyte meiosis and embryonic mitoses.
Authors: Authors: Hinkle B, Rolls MM, Stein P, Rapoport T, Terasaki M.
Zygote
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The pathway of US11-dependent degradation of MHC class I heavy chains involves a ubiquitin-conjugated intermediate.
Authors: Authors: Shamu CE, Story CM, Rapoport TA, Ploegh HL.
J Cell Biol
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Posttranslational protein translocation across the membrane of the endoplasmic reticulum.
Authors: Authors: Rapoport TA, Matlack KE, Plath K, Misselwitz B, Staeck O.
Biol Chem
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Control of glycosylation of MHC class II-associated invariant chain by translocon-associated RAMP4.
Authors: Authors: Schröder K, Martoglio B, Hofmann M, Hölscher C, Hartmann E, Prehn S, Rapoport TA, Dobberstein B.
EMBO J
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Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex.
Authors: Authors: Misselwitz B, Staeck O, Matlack KE, Rapoport TA.
J Biol Chem
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A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein.
Authors: Authors: Rolls MM, Stein PA, Taylor SS, Ha E, McKeon F, Rapoport TA.
J Cell Biol
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BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane.
Authors: Authors: Matlack KE, Misselwitz B, Plath K, Rapoport TA.
Cell
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The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex.
Authors: Authors: Meyer TH, Ménétret JF, Breitling R, Miller KR, Akey CW, Rapoport TA.
J Mol Biol
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