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

Viviana Barra, Glennis A. Logsdon, Andrea Scelfo, Sebastian Hoffmann, Solène Hervé, Aaron Aslanian, Yael Nechemia-Arbely, Don W. Cleveland, Ben E. Black and Daniele Fachinetti ()
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Viviana Barra: PSL Research University, CNRS, UMR 144
Glennis A. Logsdon: University of Pennsylvania
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
Don W. Cleveland: University of California at San Diego
Ben E. Black: University of Pennsylvania
Daniele Fachinetti: PSL Research University, CNRS, UMR 144

Nature Communications, 2019, vol. 10, issue 1, 1-10

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-018-08073-1

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