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Post‐translational modification by O‐GlcNAc: Another way to change protein function
Author(s) -
Kudlow Jeffrey E.
Publication year - 2006
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20926
Subject(s) - threonine , serine , posttranslational modification , glycosylation , chemistry , chemical modification , biochemistry , enzyme , function (biology) , intracellular , transcription (linguistics) , microbiology and biotechnology , biology , linguistics , philosophy
Modification of intracellular proteins by the β‐linkage of the monosaccharide, N‐acetylglucosamine to serine or threonine hydroxyls (O‐GlcNAc) is abundant and reversible. Although many proteins bear this post‐translational covalent modification, the changes in function of the proteins as a result of this modification are only starting to be understood. In this article, we describe how aspects of the flux from the glucose backbone to this modification are modified and how the cellular activity and content of the GC‐box binding transcription factor, Sp1, is altered by O‐glycosylation. The association of the enzyme that puts on the O‐GlcNAc modification with the bi‐functional enzyme that removes this modification is discussed relative to the transition between transcriptional repression and activation. J. Cell. Biochem. 98: 1062–1075, 2006. © 2006 Wiley‐Liss, Inc.