Thomas U. Schwartz

Thomas U. Schwartz

Boris Magasanik Professor of Biology

Thomas U. Schwartz investigates communication across biological membranes, using structural, biochemical, and genetic tools.






Sarah Wylie



Assistant Phone


  • PhD, 2000, Free University of Berlin
  • MS, 1996, Biochemistry, Free University of Berlin
  • BS, 1993, Biochemistry, Free University of Berlin

Research Summary

Our primary goal is to understand how signals and molecules are transmitted between the nucleus and cytoplasm across the nuclear envelope. We work to decipher the mechanism and structure of the machinery that executes these cellular processes.

Key Publications

  1. Structures of TorsinA and its disease-mutant complexed with an activator reveal the molecular basis for primary dystonia. Demircioglu, FE, Sosa, BA, Ingram, J, Ploegh, HL, Schwartz, TU. 2016. Elife 5, .
    doi: 10.7554/eLife.17983PMID:27490483
  2. The Nuclear Pore Complex as a Flexible and Dynamic Gate. Knockenhauer, KE, Schwartz, TU. 2016. Cell 164, 1162-1171.
    doi: 10.1016/j.cell.2016.01.034PMID:26967283
  3. Atomic structure of the Y complex of the nuclear pore. Kelley, K, Knockenhauer, KE, Kabachinski, G, Schwartz, TU. 2015. Nat Struct Mol Biol 22, 425-431.
    doi: 10.1038/nsmb.2998PMID:25822992
  4. LINC complexes form by binding of three KASH peptides to domain interfaces of trimeric SUN proteins. Sosa, BA, Rothballer, A, Kutay, U, Schwartz, TU. 2012. Cell 149, 1035-47.
    doi: 10.1016/j.cell.2012.03.046PMID:22632968
  5. Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Brohawn, SG, Leksa, NC, Spear, ED, Rajashankar, KR, Schwartz, TU. 2008. Science 322, 1369-73.
    doi: 10.1126/science.1165886PMID:18974315

Recent Publications

  1. The cellular environment shapes the nuclear pore complex architecture. Schuller, AP, Wojtynek, M, Mankus, D, Tatli, M, Kronenberg-Tenga, R, Regmi, SG, Dip, PV, Lytton-Jean, AKR, Brignole, EJ, Dasso, M et al.. 2021. Nature , .
    doi: 10.1038/s41586-021-03985-3PMID:34646014
  2. Structures of FHOD1-Nesprin1/2 complexes reveal alternate binding modes for the FH3 domain of formins. Lim, SM, Cruz, VE, Antoku, S, Gundersen, GG, Schwartz, TU. 2021. Structure 29, 540-552.e5.
    doi: 10.1016/j.str.2020.12.013PMID:33472039
  3. A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. Nordeen, SA, Andersen, KR, Knockenhauer, KE, Ingram, JR, Ploegh, HL, Schwartz, TU. 2020. Nat Commun 11, 6179.
    doi: 10.1038/s41467-020-19884-6PMID:33268786
  4. Yeast Nup84-Nup133 complex structure details flexibility and reveals conservation of the membrane anchoring ALPS motif. Nordeen, SA, Turman, DL, Schwartz, TU. 2020. Nat Commun 11, 6060.
    doi: 10.1038/s41467-020-19885-5PMID:33247142
  5. Structural Analysis of Different LINC Complexes Reveals Distinct Binding Modes. Cruz, VE, Esra Demircioglu, F, Schwartz, TU. 2020. J Mol Biol 432, 6028-6041.
    doi: 10.1016/j.jmb.2020.09.019PMID:33058875
  6. Exploring cellular biochemistry with nanobodies. Cheloha, RW, Harmand, TJ, Wijne, C, Schwartz, TU, Ploegh, HL. 2020. J Biol Chem 295, 15307-15327.
    doi: 10.1074/jbc.REV120.012960PMID:32868455
  7. Quantifying the heterogeneity of macromolecular machines by mass photometry. Sonn-Segev, A, Belacic, K, Bodrug, T, Young, G, VanderLinden, RT, Schulman, BA, Schimpf, J, Friedrich, T, Dip, PV, Schwartz, TU et al.. 2020. Nat Commun 11, 1772.
    doi: 10.1038/s41467-020-15642-wPMID:32286308
  8. The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. Demircioglu, FE, Zheng, W, McQuown, AJ, Maier, NK, Watson, N, Cheeseman, IM, Denic, V, Egelman, EH, Schwartz, TU. 2019. Nat Commun 10, 3262.
    doi: 10.1038/s41467-019-11194-wPMID:31332180
  9. Recombinant Purification of the Periplasmic Portion of the LINC Complex. Cruz, VE, Schwartz, TU. 2018. Methods Mol Biol 1840, 17-23.
    doi: 10.1007/978-1-4939-8691-0_2PMID:30141034
  10. Natively Unfolded FG Repeats Stabilize the Structure of the Nuclear Pore Complex. Onischenko, E, Tang, JH, Andersen, KR, Knockenhauer, KE, Vallotton, P, Derrer, CP, Kralt, A, Mugler, CF, Chan, LY, Schwartz, TU et al.. 2017. Cell 171, 904-917.e19.
    doi: 10.1016/j.cell.2017.09.033PMID:29033133
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