O-GlcNAc signalling: implications for cancer cell biology

Nat Rev Cancer. 2011 Aug 18;11(9):678-84. doi: 10.1038/nrc3114.

Abstract

O-GlcNAcylation is the covalent attachment of β-D-N-acetylglucosamine (GlcNAc) sugars to serine or threonine residues of nuclear and cytoplasmic proteins, and it is involved in extensive crosstalk with other post-translational modifications, such as phosphorylation. O-GlcNAcylation is becoming increasing realized as having important roles in cancer-relevant processes, such as cell signalling, transcription, cell division, metabolism and cytoskeletal regulation. However, currently little is known about the specific roles of aberrant O-GlcNAcylation in cancer. In this Opinion article, we summarize the current understanding of O-GlcNAcylation in cancer and its emerging functions in transcriptional regulation at the level of chromatin and transcription factors.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Acetylglucosamine / metabolism*
  • Acylation
  • Cell Transformation, Neoplastic
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Molecular Targeted Therapy
  • N-Acetylglucosaminyltransferases / antagonists & inhibitors
  • N-Acetylglucosaminyltransferases / chemistry
  • N-Acetylglucosaminyltransferases / metabolism*
  • Neoplasms / drug therapy
  • Neoplasms / enzymology*
  • Neoplasms / physiopathology
  • Signal Transduction*
  • Substrate Specificity

Substances

  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • Acetylglucosamine