TY - JOUR
T1 - O-Linked β-N-acetylglucosamine (O-GlcNAc) regulates emerin binding to barrier to autointegration factor (BAF) in a chromatin- and lamin B-enriched niche
AU - Berk, Jason M.
AU - Maitra, Sushmit
AU - Dawdy, Andrew W.
AU - Shabanowitz, Jeffrey
AU - Hunt, Donald F.
AU - Wilson, Katherine L.
PY - 2013/10/18
Y1 - 2013/10/18
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M113.503060
DO - 10.1074/jbc.M113.503060
M3 - Article
C2 - 24014020
AN - SCOPUS:84886896817
SN - 0021-9258
VL - 288
SP - 30192
EP - 30209
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 42
ER -