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Phosphorylation of CENP-A on serine 7 does not control centromere function

Author

Listed:
  • Viviana Barra

    (PSL Research University, CNRS, UMR 144
    Institut Gustave Roussy, CNRS UMR8200)

  • Glennis A. Logsdon

    (University of Pennsylvania
    University of Pennsylvania
    University of Washington School of Medicine)

  • Andrea Scelfo

    (PSL Research University, CNRS, UMR 144)

  • Sebastian Hoffmann

    (PSL Research University, CNRS, UMR 144)

  • Solène Hervé

    (PSL Research University, CNRS, UMR 144)

  • Aaron Aslanian

    (The Scripps Research Institute)

  • Yael Nechemia-Arbely

    (University of California at San Diego
    University of Pittsburgh Cancer Institute, School of Medicine, University of Pittsburgh)

  • Don W. Cleveland

    (University of California at San Diego)

  • Ben E. Black

    (University of Pennsylvania
    University of Pennsylvania)

  • Daniele Fachinetti

    (PSL Research University, CNRS, UMR 144)

Abstract

CENP-A is the histone H3 variant necessary to specify the location of all eukaryotic centromeres via its CENP-A targeting domain and either one of its terminal regions. In humans, several post-translational modifications occur on CENP-A, but their role in centromere function remains controversial. One of these modifications of CENP-A, phosphorylation on serine 7, has been proposed to control centromere assembly and function. Here, using gene targeting at both endogenous CENP-A alleles and gene replacement in human cells, we demonstrate that a CENP-A variant that cannot be phosphorylated at serine 7 maintains correct CENP-C recruitment, faithful chromosome segregation and long-term cell viability. Thus, we conclude that phosphorylation of CENP-A on serine 7 is dispensable to maintain correct centromere dynamics and function.

Suggested Citation

  • Viviana Barra & Glennis A. Logsdon & Andrea Scelfo & Sebastian Hoffmann & Solène Hervé & Aaron Aslanian & Yael Nechemia-Arbely & Don W. Cleveland & Ben E. Black & Daniele Fachinetti, 2019. "Phosphorylation of CENP-A on serine 7 does not control centromere function," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-08073-1
    DOI: 10.1038/s41467-018-08073-1
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    Cited by:

    1. Harsh Nagpal & Ahmad Ali-Ahmad & Yasuhiro Hirano & Wei Cai & Mario Halic & Tatsuo Fukagawa & Nikolina Sekulić & Beat Fierz, 2023. "CENP-A and CENP-B collaborate to create an open centromeric chromatin state," Nature Communications, Nature, vol. 14(1), pages 1-18, December.

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