Ubiquitous and temporal glycosylation of nuclear and cytoplasmic proteins

Gerald W. Hart, Kenneth D. Greis, L. Y.Dennis Dong, Melissa A. Blomberg, Teh Ying Chou, Man Shiow Jiang, Elizabeth P. Roquemore, Doris M. Snow, Lisa K. Kreppel, Robert C. Cole, Bradley K. Hayes

Research output: Contribution to journalArticlepeer-review

Abstract

We have described a novel form of nuclear and cytoplasmic protein glycosylation (O-GlcNAc), which is as abundant and as transient on intracellular proteins as protein phosphorylation. O-GlcNAc consists of single, non-modified N~ acetylglucosamine residues O-glycosidically attached to Ser(Thr) hydroxyl moieties at sites similar to those used by growth-factor kinases. O-GlcNAc occurs on ‘hundreds’ of intracellular proteins in all eukaryotes. Proteins bearing O-GlcNAc include cytoskeletal-, viral-, nuclear pore-, heat shock-, and transcriptional regulatory proteins. Available data suggest that O-GlcNAc is a regulatory modification that mediates subunit-subunit interactions, and in many cases blocks phosphorylation.

Original languageEnglish (US)
Pages (from-to)1637-1645
Number of pages9
JournalPure and Applied Chemistry
Volume67
Issue number10
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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