[HTML][HTML] AlternativeO-Glycosylation/O-Phosphorylation of Serine-16 in Murine Estrogen Receptor β: POST-TRANSLATIONAL REGULATION OF TURNOVER AND …
X Cheng, GW Hart - Journal of Biological Chemistry, 2001 - ASBMB
O-LinkedN-acetylglucosamine (O-GlcNAc) is a dynamic post-translational modification
abundant on nuclear and cytoplasmic proteins. Recently, we demonstrated that the murine
estrogen receptor-β (mER-β) is alternatively O-GlcNAcylated orO-phosphorylated at Ser 16.
Analyses of mER-βs containing mutations in the three adjacent hydroxyl amino acids at this
locus confirmed that Ser 16 is the major site ofO-GlcNAc modification on mER-β and that
mutants lacking hydoxyl amino acids at this locus are glycosylation-deficient. Pulse-chase …
abundant on nuclear and cytoplasmic proteins. Recently, we demonstrated that the murine
estrogen receptor-β (mER-β) is alternatively O-GlcNAcylated orO-phosphorylated at Ser 16.
Analyses of mER-βs containing mutations in the three adjacent hydroxyl amino acids at this
locus confirmed that Ser 16 is the major site ofO-GlcNAc modification on mER-β and that
mutants lacking hydoxyl amino acids at this locus are glycosylation-deficient. Pulse-chase …