title: N-Myristoyltransferase 1 interacts with calnexin at the endoplasmic reticulum.
abstract: Calnexin is a type 1 integral endoplasmic reticulum (ER) membrane molecular chaperone with a highly conserved C-terminal domain oriented to the cytoplasm. Protein N-myristoylation plays an important role in a wide variety of cellular signal transduction pathways and it is catalyzed by N-myristoyltransferase (NMT), a cytoplasmic and ER associated enzyme. Here using yeast two-hybrid screen, Western blot analysis, immunoprecipitation, immunolocalization and cellular fractionation we discovered that N-myristoyltransferase 1 interacts with calnexin at the ER. These observations point at a previously unrecognized contribution of calnexin to the retention of NMT1 at the ER membrane.
authors.affiliation: Departments of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
authors.forename: Elzbieta
authors.initials: E
authors.lastname: Dudek
authors.affiliation: Departments of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
authors.forename: Robyn
authors.initials: R
authors.lastname: Millott
authors.affiliation: Departments of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
authors.forename: Wen-Xin
authors.initials: WX
authors.lastname: Liu
authors.affiliation: Departments of Cell Biology, Faculty of Medicine & Dentistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
authors.forename: Erwan
authors.initials: E
authors.lastname: Beauchamp
authors.affiliation: Departments of Cell Biology, Faculty of Medicine & Dentistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada.
authors.forename: Luc G
authors.initials: LG
authors.lastname: Berthiaume
authors.affiliation: Departments of Biochemistry, University of Alberta, Edmonton, Alberta, T6G 2H7, Canada. Electronic address: marek.michalak@ualberta.ca.
authors.forename: Marek
authors.initials: M
authors.lastname: Michalak
mesh_terms: D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D000831:Animals, Newborn; D001665:Binding Sites; D037281:Calnexin / Q000378:metabolism*; D002478:Cells, Cultured; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D004789:Enzyme Activation; D005347:Fibroblasts / Q000378:metabolism*; D051379:Mice; D011485:Protein Binding; D013347:Subcellular Fractions / Q000378:metabolism*; D013379:Substrate Specificity; D014018:Tissue Distribution
chemical_list: D037281:Calnexin; D000217:Acyltransferases; C527098:N-myristoyltransferase, mouse
keywords: Calnexin; Endoplasmic reticulum; Myristoylation; Myristoyltransferase