ADAM and Eph: how Ephrin-signaling cells become detached

Cell. 2005 Oct 21;123(2):185-7. doi: 10.1016/j.cell.2005.10.004.

Abstract

Ephrin ligands presented on one cell surface associate with their receptors on the surface of a juxtaposed cell, often resulting in cell-cell repulsion. In this issue of Cell, Janes et al. (2005) show that the ephrin ligand can be proteolytically released from its membrane tether by a complex on the opposing cell composed of the ephrin receptor and an ADAM metalloprotease.

Publication types

  • Comment

MeSH terms

  • ADAM Proteins / chemistry
  • ADAM Proteins / genetics
  • ADAM Proteins / metabolism*
  • ADAM10 Protein
  • Amino Acid Sequence
  • Amyloid Precursor Protein Secretases
  • Crystallography, X-Ray
  • Cysteine / chemistry
  • Ephrin-A2 / metabolism*
  • Ephrin-A3 / chemistry
  • Ephrin-A3 / metabolism*
  • Ephrin-A5 / chemistry
  • Ephrin-A5 / metabolism*
  • Humans
  • Ligands
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Models, Biological
  • Molecular Sequence Data
  • Mutagenesis
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Receptor, EphA3 / metabolism
  • Sequence Homology, Amino Acid
  • Substrate Specificity

Substances

  • Ephrin-A2
  • Ephrin-A3
  • Ephrin-A5
  • Ligands
  • Membrane Proteins
  • Receptor, EphA3
  • Amyloid Precursor Protein Secretases
  • ADAM Proteins
  • ADAM10 Protein
  • ADAM10 protein, human
  • Cysteine