Phosphorylation of CENP-A on serine 7 does not control centromere function
- Autori: Barra V.; Logsdon G.A.; Scelfo A.; Hoffmann S.; Herve S.; Aslanian A.; Nechemia-Arbely Y.; Cleveland D.W.; Black B.E.; Fachinetti D.
- Anno di pubblicazione: 2019
- Tipologia: Articolo in rivista
- OA Link: http://hdl.handle.net/10447/391406
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.