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Deciphering the roles of O‐GlcNAcylation during CD4+ T‐cells activation
Author(s) -
Shimoji Shino,
Hart Gerald W
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.6.a1035
Subject(s) - cytosol , ionomycin , serine , threonine , transcription factor , signal transduction , microbiology and biotechnology , chemistry , nuclear transport , cell nucleus , phosphorylation , enzyme , nucleus , biochemistry , in vitro , biology , gene
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‐GlcNAc 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. (Supported by NIH grants CA42486 and HD13563. Dr. Hart receives a share of royalty received by the university on sales of the CTD 110.6 antibody. Terms of this arrangement are managed by JHU.)