O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched niche

Jason M. Berk, Sushmit Maitra, Andrew W. Dawdy, Jeffrey Shabanowitz, Donald F. Hunt, Katherine L. Wilson

Research output: Contribution to journalArticle

Abstract

Background: Nuclear membrane protein emerin binding to nuclear intermediate filaments (lamins) and BAF contributes to forming a nuclear "lamina" structure. Results: Emerin is O-GlcNAc-modified at eight sites: two (Ser-53 and Ser-54) influence further O-GlcNAcylation, and one (Ser-173) regulates association with BAF in the chromatin/lamin B "niche." Conclusion: O-GlcNAc transferase, a nutrient-responsive enzyme, regulates emerin. Significance: Emerin hyper-O-GlcNAcylation may contribute to cardiomyopathy and other conditions.

Original languageEnglish (US)
Pages (from-to)30192-30209
Number of pages18
JournalJournal of Biological Chemistry
Volume288
Issue number42
DOIs
StatePublished - Oct 18 2013

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched niche'. Together they form a unique fingerprint.

  • Cite this