Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins

Annu Rev Biochem. 1997;66:315-35. doi: 10.1146/annurev.biochem.66.1.315.


Modification of Ser and Thr residues by attachment of O-linked N-acetylglucos-amine [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 nuclearoncogene 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.

Publication types

  • Review

MeSH terms

  • Animals
  • Cytoskeletal Proteins / metabolism*
  • Forecasting
  • Glycosylation
  • Humans
  • Membrane Proteins / metabolism
  • Nuclear Proteins / metabolism*
  • Signal Transduction


  • Cytoskeletal Proteins
  • Membrane Proteins
  • Nuclear Proteins