Varshney Shweta, Stanley Pamela
Department of Cell Biology, Albert Einstein College of Medicine, New York, NY 10461, U.S.A.
Biochem Soc Trans. 2017 Apr 15;45(2):401-408. doi: 10.1042/BST20160165.
Here, we describe a recently discovered -GlcNAc transferase termed EOGT for EGF domain-specific -GlcNAc transferase. EOGT transfers GlcNAc (-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 -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 and humans. Mutations in EOGT that give rise to Adams-Oliver Syndrome in humans will also be discussed.
在这里，我们描述了一种最近发现的β-N-乙酰葡糖胺转移酶，称为EOGT，即表皮生长因子结构域特异性β-N-乙酰葡糖胺转移酶。EOGT将GlcNAc（N-乙酰葡糖胺）转移到分泌蛋白和膜蛋白的丝氨酸或苏氨酸上，这些蛋白含有一个或多个具有特定共有序列的表皮生长因子样重复序列。因此，EOGT不同于OGT（β-N-乙酰葡糖胺转移酶），后者将GlcNAc转移到细胞质或细胞核蛋白的丝氨酸/苏氨酸上。EOGT和OGT存在于不同的细胞区室中，并且具有大多不同的底物，尽管两者都可以作用于跨膜蛋白的细胞质（OGT）和管腔（EOGT）结构域。本综述将描述EOGT的已知底物以及EOGT在小鼠和人类中的生物学作用。还将讨论导致人类亚当斯-奥利弗综合征的EOGT突变。
