N-Myristoyltransferase 1 interacts with calnexin at the endoplasmic reticulum

Biochem Biophys Res Commun. 2015 Dec 25;468(4):889-93. doi: 10.1016/j.bbrc.2015.11.052. Epub 2015 Nov 19.

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.

Keywords: Calnexin; Endoplasmic reticulum; Myristoylation; Myristoyltransferase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acyltransferases / metabolism*
  • Animals
  • Animals, Newborn
  • Binding Sites
  • Calnexin / metabolism*
  • Cells, Cultured
  • Endoplasmic Reticulum / metabolism*
  • Enzyme Activation
  • Fibroblasts / metabolism*
  • Mice
  • Protein Binding
  • Subcellular Fractions / metabolism*
  • Substrate Specificity
  • Tissue Distribution

Substances

  • Calnexin
  • Acyltransferases
  • N-myristoyltransferase, mouse