A sweet development in Notch regulation

J Biol Chem. 2017 Sep 22;292(38):15974-15975. doi: 10.1074/jbc.H117.800102.

Abstract

The transmembrane signaling protein Notch, which is crucial for embryonic cell fate decisions, has 36 extracellular EGF domains that are glycosylated in variable and complex ways. A new study shows that O-fucose and O-glucose stabilize the repeats but that extension of glucose by xylose weakens stability, explained by the binding of the glycan to a protein groove. This work shows how different types of glycosylation can distinctly influence protein stability and structure.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Glycosylation
  • Models, Molecular
  • Protein Conformation
  • Protein Stability
  • Receptors, Notch / chemistry*
  • Receptors, Notch / metabolism*
  • Repetitive Sequences, Amino Acid
  • Signal Transduction

Substances

  • Receptors, Notch

Associated data

  • PDB/5VYG
  • PDB/4D0E