Phosphorylation of Drosophila CENP-A on serine 20 regulates protein turn-over and centromere-specific loading.

ABSTRACT: Centromeres are specialized chromosomal regions epigenetically defined by the presence of the histone H3 variant CENP-A. CENP-A is required for kinetochore formation which is essential for chromosome segregation during mitosis. Spatial restriction of CENP-A to the centromere is tightly controlled. Its overexpression results in ectopic incorporation and the formation of potentially deleterious neocentromeres in yeast, flies and in various human cancers. While the contribution of posttranslational modifications of CENP-A to these processes has been studied in yeast and mammals to some extent, very little is known about Drosophila melanogaster. Here, we show that CENP-A is phosphorylated at serine 20 (S20) by casein kinase II and that in mitotic cells, the phosphorylated form is enriched on c

SUBMITTER: Huang A 

PROVIDER: S-EPMC6847487 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature