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

• DOI: 10.1038/s41467-018-08073-1
• Publication Date: 2019-01-08T15:54:34Z
• Authors: Viviana Barra; Glennis A. Logsdon; Andrea Scelfo; Sebastian Hoffmann; Solène Hervé; Aaron Aslanian; Yael Nechemia-Arbely; Don W. Cleveland; Ben E. Black; Daniele Fachinetti
• Keywords: Gene Editing; 0301 basic medicine; 570; 1.1 Normal biological development and functioning; [SDV]Life Sciences [q-bio]; Science; Q; Centromere; 612; [SDV.BC]Life Sciences [q-bio]/Cellular Biology; Biological Sciences; Article; 03 medical and health sciences; Underpinning research; Hela Cells; Genetics; Humans; Biochemistry and Cell Biology; Generic health relevance; Phosphorylation; Centromere Protein A; Cancer; HeLa Cells

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