An extracellular region of Serrate is essential for ligand-induced cis-inhibition of Notch signaling

Development. 2013 May;140(9):2039-49. doi: 10.1242/dev.087916.

Abstract

Cell-to-cell communication via the Notch pathway is mediated between the membrane-bound Notch receptor and either of its canonical membrane-bound ligands Delta or Serrate. Notch ligands mediate receptor transactivation between cells and also mediate receptor cis-inhibition when Notch and ligand are co-expressed on the same cell. We demonstrate in Drosophila that removal of any of the EGF-like repeats (ELRs) 4, 5 or 6 results in a Serrate molecule capable of transactivating Notch but exhibiting little or no Notch cis-inhibition capacity. These forms of Serrate require Epsin (Liquid facets) to transduce a signal, suggesting that ELR 4-6-deficient ligands still require endocytosis for Notch activation. We also demonstrate that ELRs 4-6 are responsible for the dominant-negative effects of Serrate ligand forms that lack the intracellular domain and are therefore incapable of endocytosis in the ligand-expressing cell. We find that ELRs 4-6 of Serrate are conserved across species but do not appear to be conserved in Delta homologs.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adaptor Proteins, Vesicular Transport / metabolism
  • Amino Acid Sequence
  • Animals
  • Animals, Genetically Modified / genetics
  • Animals, Genetically Modified / metabolism
  • Calcium-Binding Proteins / genetics
  • Calcium-Binding Proteins / metabolism*
  • Cell Membrane / genetics
  • Cell Membrane / metabolism
  • Conserved Sequence
  • Drosophila Proteins / genetics
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Endocytosis
  • Female
  • Gene Deletion
  • Intercellular Signaling Peptides and Proteins / genetics
  • Intercellular Signaling Peptides and Proteins / metabolism*
  • Jagged-1 Protein
  • Ligands
  • Male
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Protein Binding
  • Receptors, Notch / genetics
  • Receptors, Notch / metabolism*
  • Serrate-Jagged Proteins
  • Signal Transduction
  • Transcription Factors / genetics
  • Transcription Factors / metabolism
  • Transcriptional Activation
  • Transfection
  • Transgenes
  • Wings, Animal / cytology
  • Wings, Animal / metabolism

Substances

  • Adaptor Proteins, Vesicular Transport
  • Calcium-Binding Proteins
  • Drosophila Proteins
  • GAL4 protein, Drosophila
  • Intercellular Signaling Peptides and Proteins
  • Jagged-1 Protein
  • Ligands
  • Membrane Proteins
  • N protein, Drosophila
  • Receptors, Notch
  • Ser protein, Drosophila
  • Serrate-Jagged Proteins
  • Transcription Factors
  • epsin