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Author Jiang, Kuan ♦ Bai, Bingyang ♦ Ta, Yajie ♦ Zhang, Tingling ♦ Xiao, Zikang ♦ Wang, Peng George ♦ Zhang, Lianwen
Source United States Department of Energy Office of Scientific and Technical Information
Content type Text
Language English
Subject Keyword APPLIED LIFE SCIENCES ♦ BIOLOGICAL STRESS ♦ GENE REGULATION ♦ GLUCOSAMINE ♦ LIGASES ♦ MUTATIONS ♦ STIMULATION ♦ TRANSCRIPTION ♦ TRANSFERASES
Abstract O-GlcNAc modification of cytosolic and nuclear proteins regulates essential cellular processes such as stress responses, transcription, translation, and protein degradation. Emerging evidence indicates O-GlcNAcylation has a dynamic interplay with ubiquitination in cellular regulation. Here, we report that O-GlcNAc indirectly targets a vital E3 ubiquitin ligase enzyme of NEDD4-1. The protein level of NEDD4-1 is accordingly decreased following an increase of overall O-GlcNAc level upon PUGNAc or glucosamine stimulation. O-GlcNAc transferase (OGT) knockdown, overexpression and mutation results confirm that the stability of NEDD4-1 is negatively regulated by cellular O-GlcNAc. Moreover, the NEDD4-1 degradation induced by PUGNAc or GlcN is significantly inhibited by the caspase inhibitor. Our study reveals a regulation mechanism of NEDD4-1 stability by O-GlcNAcylation. - Highlights: • Reduced NEDD4-1 correlates with increased overall O-GlcNAc level. • OGT negatively regulates NEDD4-1 stability. • O-GlcNAc regulates NEDD4-1 through caspase-mediated pathway.
ISSN 0006291X
Educational Use Research
Learning Resource Type Article
Publisher Date 2016-03-18
Publisher Place United States
Journal Biochemical and Biophysical Research Communications
Volume Number 471
Issue Number 4


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