The endoplasmic reticulum-based acetyltransferases, ATase1 and ATase2, associate with the oligosaccharyltransferase to acetylate correctly folded polypeptides.
作者： Yun Ding , Cosma D. Dellisanti , Mi Hee Ko , Cynthia Czajkowski , Luigi Puglielli
关键词:
摘要: The endoplasmic reticulum (ER) has two membrane-bound acetyltransferases responsible for the endoluminal Nϵ-lysine acetylation of ER-transiting and -resident proteins. Mutations that impair ER-based machinery are associated with developmental defects a familial form spastic paraplegia. Deficient ER in mouse leads to immune nervous system. Here, we report both ATase1 ATase2 homo- heterodimers associate members oligosaccharyltransferase (OST) complex. In contrast OST, ATases only modify correctly folded polypetides. Collectively, our studies suggest one functions is work concert OST “select” from unfolded/misfolded transiting polypeptides.
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