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Determining Role of O‐GlcNAcylation During T‐cell Activation
Author(s) -
Shimoji Shino,
Hart Gerald W
Publication year - 2008
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.22.1_supplement.826.3
Subject(s) - ionomycin , serine , threonine , signal transduction , microbiology and biotechnology , nuclear transport , chemistry , stable isotope labeling by amino acids in cell culture , phosphorylation , chromosomal translocation , nucleus , cell nucleus , biochemistry , biology , intracellular , gene , proteomics
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. Regulatory factors NFκB, NFATc1, and Elf‐1 have been identified to be O‐GlcNAc modified upon activation. O‐GlcNAcylation of Elf‐1 is necessary for translocation into nucleus. OGT expression has been positively linked to IL‐2 production. These data identify O‐GlcNAcylation as an integral part of signal transduction during T‐cell activation. We examined O‐GlcNAcylation changes upon PMA/ionomycin activation. Preliminary study showed cyto‐nuclear O‐GlcNAcylation levels increased through the first 2 hrs of the activation. The changes appeared to be protein specific. SILAC was used to identify the proteins with altered modifications. 30 proteins with increased modifications and 18 proteins with decreased modifications were identified. (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.)