@article{21762,
  abstract     = {Bacteria, like eukaryotes, use conserved cytoskeletal systems for intracellular organization. The plasmid-encoded ParMRC system forms actin-like filaments that segregate low–copy number plasmids. In multicellular cyanobacteria such as Anabaena sp., we found that a chromosomally encoded ParMR system has evolved into a cytoskeletal system named CorMR with a function in cell shape control rather than DNA segregation. Live-cell imaging, in vitro reconstitution, and cryo–electron microscopy revealed that CorM formed dynamically unstable, antiparallel double-stranded filaments that were recruited to the membrane by CorR through an amphipathic helix conserved in multicellular cyanobacteria. CorMR filaments were regulated by MinC, which excluded them from the poles and division plane. Comparative genomics indicated that the repurposing of ParMR and Min systems coevolved with cyanobacterial multicellularity, highlighting the evolutionary plasticity of cytoskeletal systems in bacteria.},
  author       = {Springstein, Benjamin L and Javoor, Manjunath and Megrian, Daniela and Hajdu, Roman and Hanke, Dustin M. and Zens, Bettina and Weiss, Gregor L. and Schur, Florian Km and Loose, Martin},
  issn         = {1095-9203},
  journal      = {Science},
  number       = {6795},
  publisher    = {AAAS},
  title        = {{Repurposing of a DNA segregation machinery into a cytoskeletal system controlling cell shape}},
  doi          = {10.1126/science.aea6343},
  volume       = {392},
  year         = {2026},
}

@misc{19915,
  author       = {Springstein, Benjamin L},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Files for "Evolutionary repurposing of a DNA segregation machinery into a cytoskeletal system controlling cyanobacterial cell shape"}},
  doi          = {10.15479/AT:ISTA:19915},
  year         = {2025},
}

@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},
}