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CEP44 ensures the formation of bona fide centriole wall, a requirement for the centriole-to-centrosome conversion

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  • Enrico S. Atorino

    (Zentrum für Molekulare Biologie, Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Shoji Hata

    (Zentrum für Molekulare Biologie, Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Charlotta Funaya

    (Electron Microscopy Core Facility, Universität Heidelberg)

  • Annett Neuner

    (Zentrum für Molekulare Biologie, Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Elmar Schiebel

    (Zentrum für Molekulare Biologie, Universität Heidelberg, DKFZ-ZMBH Allianz)

Abstract

Centrosomes are essential organelles with functions in microtubule organization that duplicate once per cell cycle. The first step of centrosome duplication is the daughter centriole formation followed by the pericentriolar material recruitment to this centriole. This maturation step was termed centriole-to-centrosome conversion. It was proposed that CEP295-dependent recruitment of pericentriolar proteins drives centriole conversion. Here we show, based on the analysis of proteins that promote centriole biogenesis, that the developing centriole structure helps drive centriole conversion. Depletion of the luminal centriole protein CEP44 that binds to the A-microtubules and interacts with POC1B affecting centriole structure and centriole conversion, despite CEP295 binding to centrioles. Impairment of POC1B, TUBE1 or TUBD1, which disturbs integrity of centriole microtubules, also prevents centriole-to-centrosome conversion. We propose that the CEP295, CEP44, POC1B, TUBE1 and TUBD1 centriole biogenesis pathway that functions in the centriole lumen and on the cytoplasmic side is essential for the centriole-to-centrosome conversion.

Suggested Citation

  • Enrico S. Atorino & Shoji Hata & Charlotta Funaya & Annett Neuner & Elmar Schiebel, 2020. "CEP44 ensures the formation of bona fide centriole wall, a requirement for the centriole-to-centrosome conversion," Nature Communications, Nature, vol. 11(1), pages 1-15, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-14767-2
    DOI: 10.1038/s41467-020-14767-2
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    Cited by:

    1. Cornelia Sala & Martin Würtz & Enrico Salvatore Atorino & Annett Neuner & Patrick Partscht & Thomas Hoffmann & Sebastian Eustermann & Elmar Schiebel, 2024. "An interaction network of inner centriole proteins organised by POC1A-POC1B heterodimer crosslinks ensures centriolar integrity," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Yutaka Takeda & Takumi Chinen & Shunnosuke Honda & Sho Takatori & Shotaro Okuda & Shohei Yamamoto & Masamitsu Fukuyama & Koh Takeuchi & Taisuke Tomita & Shoji Hata & Daiju Kitagawa, 2024. "Molecular basis promoting centriole triplet microtubule assembly," Nature Communications, Nature, vol. 15(1), pages 1-15, December.

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