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  STED nanoscopy of the centrosome linker reveals a CEP68-organized, periodic rootletin network anchored to a C-Nap1 ring at centrioles

Vlijm, R., Lic, X., Panicc, M., Rüthnickc, D., Hatac, S., Herrmannsdörfere, F., et al. (2018). STED nanoscopy of the centrosome linker reveals a CEP68-organized, periodic rootletin network anchored to a C-Nap1 ring at centrioles. Proceedings of the National Academy of Sciences of the United States of America, 115(10), E2246-E2253. doi:10.1073/pnas.1716840115.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0000-EEE0-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0000-FDA3-B
Genre: Journal Article

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 Creators:
Vlijm, Rifka1, Author              
Lic , Xue, Author
Panicc, Marko, Author
Rüthnickc, Diana, Author
Hatac, Shoji, Author
Herrmannsdörfere, Frank, Author
Kunere, Thomas, Author
Heilemanne, Mike, Author
Engelhardt, Johann2, Author              
Hell, Stefan W.2, Author              
Schiebel, Elmar, Author
Affiliations:
1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              
2Optical Nanoscopy, Max Planck Institute for Medical Research, Max Planck Society, ou_2364730              

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Free keywords: CEP68; STED superresolution; centrosome; centrosome linker; rootletin
 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

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Language(s): eng - English
 Dates: 2017-09-252018-01-212018-02-202018-02-20
 Publication Status: Published in print
 Pages: 8
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 Table of Contents: -
 Rev. Method: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proceedings of the National Academy of Sciences of the USA
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 115 (10) Sequence Number: - Start / End Page: E2246 - E2253 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230