| Literature DB >> 27518565 |
In Young Park1, Reid T Powell1, Durga Nand Tripathi1, Ruhee Dere1, Thai H Ho2, T Lynne Blasius3, Yun-Chen Chiang4, Ian J Davis5, Catherine C Fahey4, Kathryn E Hacker4, Kristen J Verhey3, Mark T Bedford6, Eric Jonasch7, W Kimryn Rathmell8, Cheryl Lyn Walker9.
Abstract
Posttranslational modifications (PTMs) of tubulin specify microtubules for specialized cellular functions and comprise what is termed a "tubulin code." PTMs of histones comprise an analogous "histone code," although the "readers, writers, and erasers" of the cytoskeleton and epigenome have heretofore been distinct. We show that methylation is a PTM of dynamic microtubules and that the histone methyltransferase SET-domain-containing 2 (SETD2), which is responsible for H3 lysine 36 trimethylation (H3K36me3) of histones, also methylates α-tubulin at lysine 40, the same lysine that is marked by acetylation on microtubules. Methylation of microtubules occurs during mitosis and cytokinesis and can be ablated by SETD2 deletion, which causes mitotic spindle and cytokinesis defects, micronuclei, and polyploidy. These data now identify SETD2 as a dual-function methyltransferase for both chromatin and the cytoskeleton and show a requirement for methylation in maintenance of genomic stability and the integrity of both the tubulin and histone codes.Entities:
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Year: 2016 PMID： 27518565 PMCID： PMC5101839 DOI： 10.1016/j.cell.2016.07.005
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582