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个人简介

• Postdoctoral associate with Prof. Watt Webb at Cornell University (2001 – 2005) • PhD from Max Planck Institute for Polymer Research and Johannes Gutenberg University of Mainz (2001) • Diploma in Chemistry from the University of Clausthal, Germany (1998)

研究领域

Biological/Chemical Physics and Physical Chemistry

Research in the Baumgart group is largely centered on the physical chemistry of amphiphile membranes with lateral heterogeneity resulting from non-ideal mixing. Our aims include characterization of biologically relevant membranes including lipids and proteins, where we investigate both composition and shape (curvature) heterogeneity. Both of these aspects are thought to be highly relevant to the function of biological membranes. We focus on freely suspended, rather than solid supported membranes, with an emphasis on bilayer membranes, but we also include monolayer systems. We investigate membranes that laterally segregate into co-existing fluid phases, and are particularly interested in quantitatively understanding the phenomenon of line tension at the phase boundary. We also examine molecular details that govern the partitioning of functionally relevant protein constructs between coexisting membrane phases and thereby aim to contribute to enhancing the biophysical understanding of transmembrane signal transduction, particularly in immune cells such as T-cells, B-cells and mast cells. Our research on aspects of membrane shape is directed at understanding how molecules sort in membrane curvature gradients. This curvature sorting likely contributes substantially to intracellular membrane sorting and trafficking. Furthermore we have recently begun to investigate phase coexistence in binary mixtures of amphiphilic di-block copolymers. Finally, we develop methods to pattern cellular signaling ligands, such as antibodies and adhesion molecules, on pattern scales both above and below optical resolution.

近期论文

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Shi Z and Baumgart T(2015). Membrane tension and peripheral protein density mediate membrane shape transitions. Nature Communications, Vol.6, Article No.5974 DOI Shen H, Giordano F, Wu Y, Chan J, Zhu C, Milosevic I, Wu X, Yao K, Chen B, Baumgart T, Sieburth D, De Camilli P.(2014). Coupling between endocytosis and sphingosine kinase 1 recruitment. Nature Cell Biology, 16(7):652-62 DOI Shi Z, and Baumgart T. (2014). Dynamics and instabilities of lipid bilayer membrane shapes. Advances in Colloid and Interface Science, 208, 76–88 DOI Chen Z, Chang K, Capraro BR, Zhu C , Hsu CJ, and Baumgart T. (2014). Intradimer / intermolecular interactions suggest auto-inhibition mechanism in endophilin A1. Journal of the American Chemical Society, 136 (12), 4557–4564 DOI Wu T, Shi Z, Baumgart T. (2014) Mutations in BIN1 associated with Central Nuclear Myopathy disrupt membrane remodeling by affecting protein density and oligomerization. PLoS ONE, 9(4): e93060 DOI Cavallaro M, Gharbi MA, Beller DA, Copar S, Shi Z, Baumgart T, Yang S, Kamien RD, Stebe KJ. (2013). Exploiting imperfections: Assembling surface colloids via bulk topological defects. PNAS, 110(47)18804–18808 DOI Zhao Y, Liu J, Yang, C, Capraro BR, Baumgart T, Bradley RP, Ramakrishnan N, Svitkina T and Guo W. (2013). Exo70 generates negative membrane curvature for morphogenesis and direction cell migration. Developmental Cell, 26 (3) 266 DOI Liao Z, Hsieh W, Baumgart T*, Dmochowski IJ*. (2013). Measuring Interactions between Polydimethylsiloxane and Serum Proteins at the Air−Water Interface. Langmuir, 29 (30), 9420. *Co-corresponding authors DOI Cavallaro M, Gharbi MA, Beller DA, Copar S, Shi Z, Kamien RD, Yang S, Baumgart T, Stebe KJ. (2013). Ring around the colloid. Soft Matter, 9 (38), 9099 DOI Capraro B, Shi Z, Wu T, Chen Z, Dunn J, Rhoades E, Baumgart T. (2013). Dimerization and membrane binding kinetics of endophilin N-BAR. Journal of Biological Chemistry, 288 (18), 12533-12543 DOI Spinler K, Tian A, Christian DA, Pantano DA, Baumgart T*, Discher D*.(2013). Dynamic Domains in Polymersomes: Mixtures of Polyanionic and Neutral Diblocks Respond More Rapidly to Changes in Calcium than to pH. Langmuir, 29 (24), 7499. *Co-corresponding authors DOI May RM, Okumura M, Hsu C, Bassiri H, Yang E, Rak G, Mace EM, Philip NH, Zhang W, Baumgart T, Orange JS, Nichols KE, Kambayashi T. (2012). Murine natural killer immunoreceptors use distinct proximal signaling complexes to direct cell function. Blood, 12, 474361 DOI Chinnapen DJF, Hsieh W, Welscher YM, Saslowsky DE, Kaoutzani L, Brandsma E, D'Auria L, Park H, Wangner JS, Drake KR, Kang M, Benjamin T, Ullman MD, Costello CE, Kenworthy AK, Baumgart T, Massol RH, Lencer WI (2012). Lipid Sorting by Ceramide Structure from Plasma Membrane to ER for the Cholera Toxin Receptor Ganglioside GM1. Developmental Cell, 23 (3), 573-586 DOI Hsieh WT, Hsu CJ, Capraro B, Wu T, Chen CM, Yang S, Baumgart T (2012). Curvature Sorting of Protein Domains on Solid-Supported Wavy Membranes. Langmuir, 28 (35), 12838–12843 DOI Sezgin E, Kaiser HJ, Baumgart T, Schwille P, Simons K, Levental I (2012). Elucidating membrane structure and protein behavior using giant plasma membrane vesicles. Nature Protocols, 7, 1042-1051 DOI Singh P, Paritosh M, Baumgart T, Das S (2012). Curvature sorting of proteins on a cylindrical lipid membrane tether connected to a lipid reservoir. Physical Review E, 85 (5), 051906 DOI Zhu C, Das SL, Baumgart T (2012). Nonlinear sorting, curvature generation, and crowding of Endophilin N-BAR on tubular membranes. Biophysical Journal, 102 (8), 1837-1845 DOI - offered free as a Featured Article Hsu CJ, Hsieh WT, Waldman A, Clarke F, Huseby ES, et al. (2012). Ligand Mobility Modulates Immunological Synapse Formation and T Cell Activation. PLoS ONE 7(2): e32398 DOI Hsu CJ, Baumgart T (2011). “Spatial Association of Signaling Proteins and F-actin Effects on Cluster Assembly Analyzed via Photoactivation Localization Microscopy in T Cells”, PLoS ONE, 6 (8): e23586 DOI Baumgart T, Capraro BC, Zhu C, Das SL (2011). “Thermodynamics and mechanics of membrane curvature generation and sensing by proteins and lipids”, Annual Reviews in Physical Chemistry, 62, 483-506 DOI

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