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- Title
Deciphering the roles of O-GlcNAcylation during CD4+ T-cells activation.
- Authors
Shimoji, Shino; Hart, Gerald W.
- Abstract
O-GlcNAcylation is a dynamic post-translational modification of serine/threonine with β-linked N-acetylglucosamine. This cyto-nuclear modification is found in all multi-cellular organisms. Previous observations during chemical activation of CD4+ T-cells showed decreasing O-GlcNAc levels on cytosolic proteins while increasing on nuclear proteins. In addition, transcription factor Elf-1 involved in T-cell activation requires O-GlcNAcylation for proper translocation into nucleus. These data indicate that O-GlcNAcylation is an integral part of signal transduction during T-cell activation. To investigate this, we examined O-GlcNAcylation changes resulting from PMA/ionomycin activation of CD4+ T-cells. O-GIcNAc levels increased for nuclear and cytosolic proteins through the first 2 hrs then decreased through 5hrs. Further more, individual bands showed unique O-GlcNAcylation level changes. The cellular localization and amount of O-GlcNAc transferase (OGT) and O-GlcNAcase (OGase) were unchanged. In vitro measured enzymatic activity of O-GlcNAcase also did not change. These data suggest that O-GlcNAc level changes during T-cell activation are due to alteration in OGT or OGase specific interactions.
- Subjects
T cells; SERINE; PROTEINS; CELLULAR signal transduction; TRANSFERASES
- Publication
FASEB Journal, 2007, Vol 21, Issue 6, pA1035
- ISSN
0892-6638
- Publication type
Article
- DOI
10.1096/fasebj.21.6.a1035