EOGT and O-GlcNAc on secreted and membrane proteins

Biochem Soc Trans. 2017 Apr 15;45(2):401-408. doi: 10.1042/BST20160165.

Abstract

Here, we describe a recently discovered O-GlcNAc transferase termed EOGT for EGF domain-specific O-GlcNAc transferase. EOGT transfers GlcNAc (N-acetylglucosamine) to Ser or Thr in secreted and membrane proteins that contain one or more epidermal growth factor-like repeats with a specific consensus sequence. Thus, EOGT is distinct from OGT, the O-GlcNAc transferase, that transfers GlcNAc to Ser/Thr in proteins of the cytoplasm or nucleus. EOGT and OGT are in separate cellular compartments and have mostly distinct substrates, although both can act on cytoplasmic (OGT) and lumenal (EOGT) domains of transmembrane proteins. The present review will describe known substrates of EOGT and biological roles for EOGT in Drosophila and humans. Mutations in EOGT that give rise to Adams-Oliver Syndrome in humans will also be discussed.

Keywords: EOGT; O-GlcNAc; membrane proteins; secreted proteins.

Publication types

  • Review
  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylglucosamine / metabolism
  • Animals
  • Drosophila Proteins / chemistry
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / chemistry
  • Drosophila melanogaster / enzymology*
  • Ectodermal Dysplasia / genetics*
  • Gene Expression Regulation, Developmental
  • Humans
  • Limb Deformities, Congenital / genetics*
  • Mutation
  • N-Acetylglucosaminyltransferases / chemistry
  • N-Acetylglucosaminyltransferases / genetics
  • N-Acetylglucosaminyltransferases / metabolism*
  • Protein Domains
  • Scalp Dermatoses / congenital*
  • Scalp Dermatoses / genetics
  • Signal Transduction
  • Substrate Specificity

Substances

  • Drosophila Proteins
  • EOGT protein, human
  • Eogt protein, Drosophila
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • Acetylglucosamine

Supplementary concepts

  • Adams Oliver syndrome