Ceramide synthases: roles in cell physiology and signaling

Adv Exp Med Biol. 2010;688:60-71. doi: 10.1007/978-1-4419-6741-1_4.


Ceramide synthases (CerS) are integral membrane proteins of the endoplasmic reticulum. Six mammalian CerS have been described, with each utilizing fatty acyl CoAs of relatively defined chain lengths for N-acylation of the sphingoid long chain base. In this chapter, we review the main functional features of the CerS proteins, discuss their fatty acid specificity, kinetics, tissue distribution and mode of inhibition, as well as possible posttranslational modifications. We then address the reason that mammals contain six distinct CerS, whereas most other enzymes in the sphingolipid biosynthetic pathway only occur in one or two isoforms. Finally, we discuss the putative roles of CerS and the ceramide derived from the CerS, in signaling pathways and in development of disease.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Ceramides / biosynthesis*
  • Enzyme Inhibitors / pharmacology
  • Fumonisins / pharmacology
  • Humans
  • Kinetics
  • Molecular Sequence Data
  • Oxidoreductases / antagonists & inhibitors
  • Oxidoreductases / classification
  • Oxidoreductases / genetics
  • Oxidoreductases / metabolism*
  • Phylogeny
  • Protein Processing, Post-Translational
  • Sequence Homology, Amino Acid
  • Signal Transduction
  • Substrate Specificity
  • Tissue Distribution


  • Ceramides
  • Enzyme Inhibitors
  • Fumonisins
  • Oxidoreductases
  • dihydroceramide desaturase