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

ABSTRACT: CENP-A is the histone H3 variant necessary to specify the location of all eukaryoticcentromeres 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.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: ANDREA SCELFO

LAB HEAD: Daniele Fachinetti

PROVIDER: PXD012163 | Pride | 2019-01-28

REPOSITORIES: Pride

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			Action	DRS
	CHROLATEG1_120928.zip	Other
	CHROLATEG1_120928_DTASelect.txt	Txt
	DTASelect_titaniumdioxide_rc_chromatin_2_82745.txt	Txt
	DTASelect_titaniumdioxide_sg2_chromatin_2_82746.txt	Txt
	SOLMIDS_121006.zip	Other

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Publications

[A hybrid approach to hypoplastic left heart syndrome].

Serrano-Martínez Félix F Caffarena-Calvar José M JM

Revista espanola de cardiologia 20080401 4

PMID: 18405531

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