EOGT and O-GlcNAc on secreted and membrane proteins

Shweta Varshney, Pamela Stanley

Research output: Contribution to journalReview article

14 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)401-408
Number of pages8
JournalBiochemical Society Transactions
Volume45
Issue number2
DOIs
StatePublished - Apr 15 2017

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'EOGT and O-GlcNAc on secreted and membrane proteins'. Together they form a unique fingerprint.

  • Cite this