Tomas Kirchhausen, Ph.D.

Tomas Kirchhausen, Ph.D.

Senior Investigator, Program in Cellular and Molecular Medicine (Boston Children's Hospital)
Springer Family Professor of Pediatrics (HMS)
Professor of Cell Biology (HMS)

The Kirchhausen Lab focuses on understanding processes that mediate and regulate cellular membrane remodeling, the biogenesis of organelles, and the ways by which viruses, biologicals and oligonucleotides are delivered to the cell interior. 

By direct observation of molecular events obtained using Lattice Light Sheet Microscopy and Lattice Light Sheet Microscopy optimized with Adaptive Optics (AO-LLSM), frontier optical-imaging modalities with high temporal resolution and spatial precision, we aim to bridge the gap between molecules and cells, either as independent entities in culture, as components of organoids, or as constituents of living tissues. The richness and magnitude of the big-data obtained over periods ranging from seconds to hours create new challenges for obtaining quantitative representations of the observed dynamics and for deriving accurate and comprehensive models for the underlying developmental mechanisms. With these type of dynamic studies we expect to integrate molecular snapshots obtained at molecular and atomic resolution using cryoEM with live-cell processes, in an effort to generate ‘molecular movies' allowing us to obtain frameworks for analyzing some of the molecular contacts and switches that participate in the regulation, availability, and intracellular traffic of the many molecules involved in signal transduction, immune responsiveness, lipid homeostasis, cell-cell recognition and organelle biogenesis. Such biological phenomena have importance for our understanding of many diseases including cancer, viral infection and pathogen invasion, Alzheimer's, as well as other neurological diseases.

Harvard Medical School

Dept. of Cell Biology, WAB-133

200 Longwood Avenue

Boston, MA 02115

Lab telephone: 617-713-8888

Lab fax: 617-713-8898

Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.
Authors: Authors: ter Haar E, Musacchio A, Harrison SC, Kirchhausen T.
Cell
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A dileucine motif in HIV-1 Nef is essential for sorting into clathrin-coated pits and for downregulation of CD4.
Authors: Authors: Greenberg M, DeTulleo L, Rapoport I, Skowronski J, Kirchhausen T.
Curr Biol
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Vesicle formation: dynamic dynamin lives up to its name.
Authors: Authors: Kirchhausen T.
Curr Biol
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A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.
Authors: Authors: Sanderfoot AA, Ahmed SU, Marty-Mazars D, Rapoport I, Kirchhausen T, Marty F, Raikhel NV.
Proc Natl Acad Sci U S A
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The clathrin endocytic pathway in viral infection.
Authors: Authors: DeTulleo L, Kirchhausen T.
EMBO J
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The neural cell adhesion molecule L1 interacts with the AP-2 adaptor and is endocytosed via the clathrin-mediated pathway.
Authors: Authors: Kamiguchi H, Long KE, Pendergast M, Schaefer AW, Rapoport I, Kirchhausen T, Lemmon V.
J Neurosci
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Wiskott-Aldrich syndrome: a gene, a multifunctional protein and the beginnings of an explanation.
Authors: Authors: Kirchhausen T.
Mol Med Today
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Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site.
Authors: Authors: Rapoport I, Chen YC, Cupers P, Shoelson SE, Kirchhausen T.
EMBO J
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Assembly of clathrin coats disrupts the association between Eps15 and AP-2 adaptors.
Authors: Authors: Cupers P, Jadhav AP, Kirchhausen T.
J Biol Chem
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Interaction of the bovine papillomavirus E6 protein with the clathrin adaptor complex AP-1.
Authors: Authors: Tong X, Boll W, Kirchhausen T, Howley PM.
J Virol
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