Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article Full Text Full Text (PDF, 4864K) PDF+supp data (7139K) PPT slides of all figures Supplemental Material Alert me when this article is cited Citation Map Services Email this article Similar articles in this journal Similar articles in PubMed Alert me to new content in the JCB Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Google Scholar Articles by Hall, L. L. Articles by Lawrence, J. B. PubMed PubMed Citation Articles by Hall, L. L. Articles by Lawrence, J. B. Related Collections Related Article Social Bookmarking                            What's this?

AURKB-mediated effects on chromatin regulate binding versus release of XIST RNA to the inactive chromosome

Department of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655

Correspondence to Lisa L. Hall: Lisa.Hall{at}umassmed.edu; or Jeanne B. Lawrence: Jeanne.Lawrence{at}umassmed.edu

How XIST RNA strictly localizes across the inactive X chromosome is unknown; however, prophase release of human XIST RNA provides a clue. Tests of inhibitors that mimic mitotic chromatin modifications implicated an indirect role of PP1 (protein phosphatase 1), potentially via its interphase repression of Aurora B kinase (AURKB), which phosphorylates H3 and chromosomal proteins at prophase. RNA interference to AURKB causes mitotic retention of XIST RNA, unlike other mitotic or broad kinase inhibitors. Thus, AURKB plays an unexpected role in regulating RNA binding to heterochromatin, independent of mechanics of mitosis. H3 phosphorylation (H3ph) was shown to precede XIST RNA release, whereas results exclude H1ph involvement. Of numerous Xi chromatin (chromosomal protein) hallmarks, ubiquitination closely follows XIST RNA retention or release. Surprisingly, H3S10ph staining (but not H3S28ph) is excluded from Xi and is potentially linked to ubiquitination. Results suggest a model of multiple distinct anchor points for XIST RNA. This study advances understanding of RNA chromosome binding and the roles of AURKB and demonstrates a novel approach to manipulate and study XIST RNA.

Abbreviations used in this paper: AURKB, Aurora B kinase; CANTH, cantharidin; CPC, chromosomal passenger complex; HESP, Hesperadin; IF, immunofluorescence; INCENP, inner centromere protein; NOC, nocodazole; OKA, okadaic acid; SB, sodium butyrate; STSP, staurosporine; TAUT, tautomycin; TSA, trichostatin-A.

© 2009 Hall et al.
This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

CiteULike

Complore

Connotea

Del.icio.us

Digg

Facebook

Reddit

Technorati

Twitter

This article has been cited by other articles:

• Short, B. (2009). Aurora B answers an XIST-ential question. JCB 186: 449-449 [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents