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.
journal_name
Biochem Soc Transjournal_title
Biochemical Society transactionsauthors
Varshney S,Stanley Pdoi
10.1042/BST20160165subject
Has Abstractpub_date
2017-04-15 00:00:00pages
401-408issue
2eissn
0300-5127issn
1470-8752pii
BST20160165journal_volume
45pub_type
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