Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins

Gerald Warren Hart

Research output: Contribution to journalArticlepeer-review


Modification of Ser and Thr residues by attachment of O-linked N- acetylglucosamine [Ser(Thr)-O-GlcNAcylation] to eukaryotic nuclear and cytosolic proteins is as dynamic and possibly as abundant as Ser(Thr) phosphorylation. Known O-GlcNAcylated proteins include cytoskeletal proteins and their regulatory proteins; viral proteins; nuclear-pore, heat-shock, tumor-suppressor, and nuclear-oncogene proteins; RNA polymerase II catalytic subunit; and a multitude of transcription factors. Although functionally diverse, all of these proteins are also phosphoproteins. Most O-GlcNAcylated proteins form highly regulated multimeric associations that are dependent upon their posttranslational modifications. Evidence is mounting that O- GlcNAcylation is an important regulatory modification that may have a reciprocal relationship with O-phosphorylation and may modulate many biological processes in eukaryotes.

Original languageEnglish (US)
Pages (from-to)315-335
Number of pages21
JournalAnnual Review of Biochemistry
StatePublished - 1997
Externally publishedYes


  • Cytoskeleton
  • N-acetylglucosamine
  • Nucleus
  • O-linked sugar
  • Protein glycosylation

ASJC Scopus subject areas

  • Biochemistry

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