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@ARTICLE{Vlijm:132762,
      author       = {R. Vlijm$^*$ and X. Li and M. Panic and D. Rüthnick and S.
                      Hata and F. Herrmannsdörfer and T. Kuner and M. Heilemann
                      and J. Engelhardt$^*$ and S. W. Hell$^*$ and E. Schiebel},
      title        = {{STED} nanoscopy of the centrosome linker reveals a
                      {CEP}68-organized, periodic rootletin network anchored to a
                      {C}-{N}ap1 ring at centrioles.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {115},
      number       = {10},
      issn         = {1091-6490},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DKFZ-2018-00415},
      pages        = {E2246 - E2253},
      year         = {2018},
      note         = {DKFZ-ZMBH-Allianz},
      abstract     = {The centrosome linker proteins C-Nap1, rootletin, and CEP68
                      connect the two centrosomes of a cell during interphase into
                      one microtubule-organizing center. This coupling is
                      important for cell migration, cilia formation, and timing of
                      mitotic spindle formation. Very little is known about the
                      structure of the centrosome linker. Here, we used stimulated
                      emission depletion (STED) microscopy to show that each
                      C-Nap1 ring at the proximal end of the two centrioles
                      organizes a rootletin ring and, in addition, multiple
                      rootletin/CEP68 fibers. Rootletin/CEP68 fibers originating
                      from the two centrosomes form a web-like, interdigitating
                      network, explaining the flexible nature of the centrosome
                      linker. The rootletin/CEP68 filaments are repetitive and
                      highly ordered. Staggered rootletin molecules (N-to-N and
                      C-to-C) within the filaments are 75 nm apart. Rootletin
                      binds CEP68 via its C-terminal spectrin repeat-containing
                      region in 75-nm intervals. The N-to-C distance of two
                      rootletin molecules is ∼35 to 40 nm, leading to an
                      estimated minimal rootletin length of ∼110 nm. CEP68 is
                      important in forming rootletin filaments that branch off
                      centrioles and to modulate the thickness of rootletin
                      fibers. Thus, the centrosome linker consists of a vast
                      network of repeating rootletin units with C-Nap1 as ring
                      organizer and CEP68 as filament modulator.},
      cin          = {E190},
      ddc          = {000},
      cid          = {I:(DE-He78)E190-20160331},
      pnm          = {315 - Imaging and radiooncology (POF3-315)},
      pid          = {G:(DE-HGF)POF3-315},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29463719},
      pmc          = {pmc:PMC5873239},
      doi          = {10.1073/pnas.1716840115},
      url          = {https://inrepo02.dkfz.de/record/132762},
}