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

Viviana Barra, Yael Nechemia-Arbely, Don W. Cleveland, Andrea Scelfo, Viviana Barra, Ben E. Black, Glennis A. Logsdon, Solène Hervé, Sebastian Hoffmann, Daniele Fachinetti, Daniele Fachinetti, Aaron Aslanian

Risultato della ricerca: Articlepeer review

15 Citazioni (Scopus)


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.
Lingua originaleEnglish
pagine (da-a)1-10
Numero di pagine10
RivistaNature Communications
Stato di pubblicazionePublished - 2019

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1300.1300???
  • ???subjectarea.asjc.3100.3100???


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