title: The endoplasmic reticulum-based acetyltransferases, ATase1 and ATase2, associate with the oligosaccharyltransferase to acetylate correctly folded polypeptides.
abstract: The endoplasmic reticulum (ER) has two membrane-bound acetyltransferases responsible for the endoluminal N(ϵ)-lysine acetylation of ER-transiting and -resident proteins. Mutations that impair the ER-based acetylation machinery are associated with developmental defects and a familial form of spastic paraplegia. Deficient ER acetylation in the mouse leads to defects of the immune and nervous system. Here, we report that both ATase1 and ATase2 form homo- and heterodimers and associate with members of the oligosaccharyltransferase (OST) complex. In contrast to the OST, the ATases only modify correctly folded polypetides. Collectively, our studies suggest that one of the functions of the ATases is to work in concert with the OST and "select" correctly folded from unfolded/misfolded transiting polypeptides.
authors.affiliation: Departments of Medicine and University of Wisconsin-Madison, Madison, Wisconsin 53705; Departments of Neuroscience Training Program, University of Wisconsin-Madison, Madison, Wisconsin 53705 and.
authors.forename: Yun
authors.initials: Y
authors.lastname: Ding
authors.affiliation: Departments of Neuroscience and University of Wisconsin-Madison, Madison, Wisconsin 53705.
authors.forename: Cosma D
authors.initials: CD
authors.lastname: Dellisanti
authors.affiliation: Departments of Medicine and University of Wisconsin-Madison, Madison, Wisconsin 53705.
authors.forename: Mi Hee
authors.initials: MH
authors.lastname: Ko
authors.affiliation: Departments of Neuroscience Training Program, University of Wisconsin-Madison, Madison, Wisconsin 53705 and; Departments of Neuroscience and University of Wisconsin-Madison, Madison, Wisconsin 53705.
authors.forename: Cynthia
authors.initials: C
authors.lastname: Czajkowski
authors.affiliation: Departments of Medicine and University of Wisconsin-Madison, Madison, Wisconsin 53705; Departments of Neuroscience Training Program, University of Wisconsin-Madison, Madison, Wisconsin 53705 and; Geriatric Research Education Clinical Center, Veterans Affairs Medical Center, Madison, Wisconsin 53705. Electronic address: lp1@medicine.wisc.edu.
authors.forename: Luigi
authors.initials: L
authors.lastname: Puglielli
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000737:chemistry*; D000818:Animals; D001408:Bacillus anthracis / Q000201:enzymology; D001412:Bacillus subtilis / Q000201:enzymology; D001483:Base Sequence; D004721:Endoplasmic Reticulum / Q000201:enzymology*; D004926:Escherichia coli / Q000201:enzymology; D006023:Glycoproteins / Q000737:chemistry; D006602:Hexosyltransferases / Q000737:chemistry*; D006801:Humans; D008239:Lysine / Q000737:chemistry; D008565:Membrane Proteins / Q000737:chemistry*; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D012477:Salmonella enteritidis / Q000201:enzymology
chemical_list: D006023:Glycoproteins; D008565:Membrane Proteins; D010455:Peptides; D000123:Acetyltransferases; C116373:NAT8 protein, human; C084723:acetyl-CoA - lysine N6-acetyltransferase; D006602:Hexosyltransferases; C025620:dolichyl-diphosphooligosaccharide - protein glycotransferase; D008239:Lysine
keywords: Acetyl Coenzyme A (acetyl-CoA); Acetyltransferase; Endoplasmic Reticulum (ER); Oligosaccharyltransferase; Post-translational Modification (PTM)