Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins.
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.
Hart
G W
GW
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, School of Medicine 35294-0005, USA. gwhart@bmg.bhs.uab.edu
D000818:Animals; D003598:Cytoskeletal Proteins / Q000378:metabolism*; D005544:Forecasting; D006031:Glycosylation; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D015398:Signal Transduction
D003598:Cytoskeletal Proteins; D008565:Membrane Proteins; D009687:Nuclear Proteins