| Literature DB >> 19250906 |
Rebecca J Loomis1, Yoshinori Naoe, J Brandon Parker, Velibor Savic, Matthew R Bozovsky, Todd Macfarlan, James L Manley, Debabrata Chakravarti.
Abstract
Histone H3 serine 10 phosphorylation is a hallmark of mitotic chromosomes, but its full function remains to be elucidated. We report here that two SR protein splicing factors, SRp20 and ASF/SF2, associate with interphase chromatin, are released from hyperphosphorylated mitotic chromosomes, but reassociate with chromatin late in M-phase. Inhibition of Aurora B kinase diminished histone H3 serine 10 phosphorylation and increased SRp20 and ASF/SF2 retention on mitotic chromosomes. Unexpectedly, we also found that HP1 proteins interact with ASF/SF2 in mitotic cells. Strikingly, siRNA-mediated knockdown of ASF/SF2 caused retention of HP1 proteins on mitotic chromatin. Finally, ASF/SF2-depleted cells released from a mitotic block displayed delayed G0/G1 entry, suggesting a functional consequence of these interactions. These findings underscore the evolving role of histone H3 phosphorylation and demonstrate a direct, functional, and histone-modification-regulated association of SRp20 and ASF/SF2 with chromatin.Entities:
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Year: 2009 PMID： 19250906 PMCID： PMC2667802 DOI： 10.1016/j.molcel.2009.02.003
Source DB: PubMed Journal: Mol Cell ISSN： 1097-2765 Impact factor: 17.970