Education
- 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
- 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 - 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 - 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 - 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 - 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
- HIV-1 capsids enter the FG phase of nuclear pores like a transport receptor. Fu, L, Weiskopf, EN, Akkermans, O, Swanson, NA, Cheng, S, Schwartz, TU, Görlich, D. 2024. Nature 626, 843-851.
doi: 10.1038/s41586-023-06966-wPMID:38267583 - FHODs: Nuclear tethered formins for nuclear mechanotransduction. Antoku, S, Schwartz, TU, Gundersen, GG. 2023. Front Cell Dev Biol 11, 1160219.
doi: 10.3389/fcell.2023.1160219PMID:37215084 - Structure and specificity of an anti-chloramphenicol single domain antibody for detection of amphenicol residues. Swofford, CA, Nordeen, SA, Chen, L, Desai, MM, Chen, J, Springs, SL, Schwartz, TU, Sinskey, AJ. 2022. Protein Sci 31, e4457.
doi: 10.1002/pro.4457PMID:36153664 - Solving the nuclear pore puzzle. Schwartz, TU. 2022. Science 376, 1158-1159.
doi: 10.1126/science.abq4792PMID:35679398 - Nanobodies as allosteric modulators of Parkinson's disease-associated LRRK2. Singh, RK, Soliman, A, Guaitoli, G, Störmer, E, von Zweydorf, F, Dal Maso, T, Oun, A, Van Rillaer, L, Schmidt, SH, Chatterjee, D et al.. 2022. Proc Natl Acad Sci U S A 119, .
doi: 10.1073/pnas.2112712119PMID:35217606 - 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 598, 667-671.
doi: 10.1038/s41586-021-03985-3PMID:34646014 - 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 - 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 - 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 - 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