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.
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