Fatty acyl CoA-mediated inhibition of endoplasmic reticulum assembly.
The protein machinery that mediates homotypic fusion of mammalian endoplasmic reticulum (ER) membranes is becoming increasing well defined. However, little is known of how acylation of constituent membrane components might impact upon this event. This is particularly important as acylation has been shown to promote both fusion and fission of heterotypic membranes. Using a previously characterised cell-free ER fusion assay, I show here that incubation of membranes in the presence of either palmitoyl CoA or myristoyl CoA potently inhibits assembly. Furthermore, inhibition does not occur when membranes are incubated in the constituent palmitate or CoA moieties alone. These findings suggest that not only do palmitoyl CoA and myristoyl CoA inhibit ER assembly, but that they might instead be functioning to actively facilitate ER membrane fission.
Turner
Mark D
MD
Centre for Diabetes and Metabolic Medicine, Institute of Cell and Molecular Science, St. Bartholomew's and The Royal London School of Medicine and Dentistry, Queen Mary, University of London, Whitechapel, London, E1 1BB, UK. M.D.Turner@qmul.ac.uk
D000215:Acylation; D003065:Coenzyme A / Q000502:physiology*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D005227:Fatty Acids / Q000378:metabolism*
D005227:Fatty Acids; D003065:Coenzyme A