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

Actin dynamics counteract membrane tension during clathrin-mediated endocytosis.
Authors: Authors: Boulant S, Kural C, Zeeh JC, Ubelmann F, Kirchhausen T.
Nat Cell Biol
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Formation of the postmitotic nuclear envelope from extended ER cisternae precedes nuclear pore assembly.
Authors: Authors: Lu L, Ladinsky MS, Kirchhausen T.
J Cell Biol
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Perforin pores in the endosomal membrane trigger the release of endocytosed granzyme B into the cytosol of target cells.
Authors: Authors: Thiery J, Keefe D, Boulant S, Boucrot E, Walch M, Martinvalet D, Goping IS, Bleackley RC, Kirchhausen T, Lieberman J.
Nat Immunol
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Redistribution of caveolae during mitosis.
Authors: Authors: Boucrot E, Howes MT, Kirchhausen T, Parton RG.
J Cell Sci
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ARFGAP1 promotes AP-2-dependent endocytosis.
Authors: Authors: Bai M, Gad H, Turacchio G, Cocucci E, Yang JS, Li J, Beznoussenko GV, Nie Z, Luo R, Fu L, Collawn JF, Kirchhausen T, Luini A, Hsu VW.
Nat Cell Biol
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Single-molecule analysis of a molecular disassemblase reveals the mechanism of Hsc70-driven clathrin uncoating.
Authors: Authors: Böcking T, Aguet F, Harrison SC, Kirchhausen T.
Nat Struct Mol Biol
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Structural analysis of the interaction between Dishevelled2 and clathrin AP-2 adaptor, a critical step in noncanonical Wnt signaling.
Authors: Authors: Yu A, Xing Y, Harrison SC, Kirchhausen T.
Structure
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The length of vesicular stomatitis virus particles dictates a need for actin assembly during clathrin-dependent endocytosis.
Authors: Authors: Cureton DK, Massol RH, Whelan SP, Kirchhausen T.
PLoS Pathog
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Structure of the PTEN-like region of auxilin, a detector of clathrin-coated vesicle budding.
Authors: Authors: Guan R, Dai H, Han D, Harrison SC, Kirchhausen T.
Structure
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Structural biology: Conservation in vesicle coats.
Authors: Authors: Harrison SC, Kirchhausen T.
Nature
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