@article{20370,
  abstract     = {The Huntingtin protein (HTT), named for its role in Huntington’s disease, has been best understood as a scaffolding protein that promotes vesicle transport by molecular motors along microtubules. Here, we show that HTT also interacts with the actin cytoskeleton, and its loss of function disturbs the morphology and function of the axonal growth cone. We demonstrate that HTT organizes F-actin into bundles. Cryo–electron tomography (cryo-ET) and subtomogram averaging (STA) structural analyses reveal that HTT’s N-terminal HEAT and Bridge domains wrap around F-actin, while the C-terminal HEAT domain is displaced; furthermore, HTT dimerizes via the N-HEAT domain to bridge parallel actin filaments separated by ~20 nanometers. Our study provides the structural basis for understanding how HTT interacts with and organizes the actin cytoskeleton.},
  author       = {Carpentier, Rémi and Kim, Jaesung and Capizzi, Mariacristina and Kim, Hyeongju and Fäßler, Florian and Hansen, Jesse and Kim, Min Jeong and Denarier, Eric and Blot, Béatrice and Degennaro, Marine and Labou, Sophia and Arnal, Isabelle and Marcaida, Maria J. and Peraro, Matteo Dal and Kim, Doory and Schur, Florian KM and Song, Ji-Joon and Humbert, Sandrine},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {38},
  publisher    = {AAAS},
  title        = {{Structure of the Huntingtin F-actin complex reveals its role in cytoskeleton organization}},
  doi          = {10.1126/sciadv.adw4124},
  volume       = {11},
  year         = {2025},
}

@article{15146,
  abstract     = {The extracellular matrix (ECM) serves as a scaffold for cells and plays an essential role in regulating numerous cellular processes, including cell migration and proliferation. Due to limitations in specimen preparation for conventional room-temperature electron microscopy, we lack structural knowledge on how ECM components are secreted, remodeled, and interact with surrounding cells. We have developed a 3D-ECM platform compatible with sample thinning by cryo-focused ion beam milling, the lift-out extraction procedure, and cryo-electron tomography. Our workflow implements cell-derived matrices (CDMs) grown on EM grids, resulting in a versatile tool closely mimicking ECM environments. This allows us to visualize ECM for the first time in its hydrated, native context. Our data reveal an intricate network of extracellular fibers, their positioning relative to matrix-secreting cells, and previously unresolved structural entities. Our workflow and results add to the structural atlas of the ECM, providing novel insights into its secretion and assembly.},
  author       = {Zens, Bettina and Fäßler, Florian and Hansen, Jesse and Hauschild, Robert and Datler, Julia and Hodirnau, Victor-Valentin and Zheden, Vanessa and Alanko, Jonna H and Sixt, Michael K and Schur, Florian KM},
  issn         = {1540-8140},
  journal      = {Journal of Cell Biology},
  number       = {6},
  publisher    = {Rockefeller University Press},
  title        = {{Lift-out cryo-FIBSEM and cryo-ET reveal the ultrastructural landscape of extracellular matrix}},
  doi          = {10.1083/jcb.202309125},
  volume       = {223},
  year         = {2024},
}

@article{14979,
  abstract     = {Poxviruses are among the largest double-stranded DNA viruses, with members such as variola virus, monkeypox virus and the vaccination strain vaccinia virus (VACV). Knowledge about the structural proteins that form the viral core has remained sparse. While major core proteins have been annotated via indirect experimental evidence, their structures have remained elusive and they could not be assigned to individual core features. Hence, which proteins constitute which layers of the core, such as the palisade layer and the inner core wall, has remained enigmatic. Here we show, using a multi-modal cryo-electron microscopy (cryo-EM) approach in combination with AlphaFold molecular modeling, that trimers formed by the cleavage product of VACV protein A10 are the key component of the palisade layer. This allows us to place previously obtained descriptions of protein interactions within the core wall into perspective and to provide a detailed model of poxvirus core architecture. Importantly, we show that interactions within A10 trimers are likely generalizable over members of orthopox- and parapoxviruses.},
  author       = {Datler, Julia and Hansen, Jesse and Thader, Andreas and Schlögl, Alois and Bauer, Lukas W and Hodirnau, Victor-Valentin and Schur, Florian KM},
  issn         = {1545-9985},
  journal      = {Nature Structural & Molecular Biology},
  keywords     = {Molecular Biology, Structural Biology},
  pages        = {1114--1123},
  publisher    = {Springer Nature},
  title        = {{Multi-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores}},
  doi          = {10.1038/s41594-023-01201-6},
  volume       = {31},
  year         = {2024},
}