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

A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles.
Authors: Authors: Søgaard M, Tani K, Ye RR, Geromanos S, Tempst P, Kirchhausen T, Rothman JE, Söllner T.
Cell
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The Saccharomyces cerevisiae APS1 gene encodes a homolog of the small subunit of the mammalian clathrin AP-1 complex: evidence for functional interaction with clathrin at the Golgi complex.
Authors: Authors: Phan HL, Finlay JA, Chu DS, Tan PK, Kirchhausen T, Payne GS.
EMBO J
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Arrangement of domains, and amino acid residues required for binding of vascular cell adhesion molecule-1 to its counter-receptor VLA-4 (alpha 4 beta 1).
Authors: Authors: Osborn L, Vassallo C, Browning BG, Tizard R, Haskard DO, Benjamin CD, Dougas I, Kirchhausen T.
J Cell Biol
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The beta 1 and beta 2 subunits of the AP complexes are the clathrin coat assembly components.
Authors: Authors: Gallusser A, Kirchhausen T.
EMBO J
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Immunoelectron microscopic evidence for the extended conformation of light chains in clathrin trimers.
Authors: Authors: Kirchhausen T, Toyoda T.
J Biol Chem
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Location of the domains of ICAM-1 by immunolabeling and single-molecule electron microscopy.
Authors: Authors: Kirchhausen T, Staunton DE, Springer TA.
J Leukoc Biol
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The medium chains of the mammalian clathrin-associated proteins have a homolog in yeast.
Authors: Authors: Nakayama Y, Goebl M, O'Brine Greco B, Lemmon S, Pingchang Chow E, Kirchhausen T.
Eur J Biochem
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AP17 and AP19, the mammalian small chains of the clathrin-associated protein complexes show homology to Yap17p, their putative homolog in yeast.
Authors: Authors: Kirchhausen T, Davis AC, Frucht S, Greco BO, Payne GS, Tubb B.
J Biol Chem
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Clathrin domains involved in recognition by assembly protein AP-2.
Authors: Authors: Keen JH, Beck KA, Kirchhausen T, Jarrett T.
J Biol Chem
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Stabilization of clathrin coats by the core of the clathrin-associated protein complex AP-2.
Authors: Authors: Matsui W, Kirchhausen T.
Biochemistry
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