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Annu Rev Biochem. 1997;66:315-35.

Dynamic O-linked glycosylation of nuclear and cytoskeletal proteins.

Author information

1
Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, School of Medicine 35294-0005, USA. gwhart@bmg.bhs.uab.edu

Abstract

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.

[Indexed for MEDLINE]

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