The role of proteases in regulating Eph/ephrin signaling

Proteases regulate a myriad of cell functions, both in normal and disease states. In addition to protein turnover, they regulate a range of signaling processes, including those mediated by Eph receptors and their ephrin ligands. A variety of proteases is reported to directly cleave Ephs and/or ephri...

Full description

Saved in:
Bibliographic Details
Published in:Cell adhesion & migration 2014-07, Vol.8 (4), p.294-307
Main Authors: Atapattu, Lakmali, Lackmann, Martin, Janes, Peter W
Format: Article
Language:English
Subjects:
ADAM
Animals
Cell Adhesion
Cell Communication
Cell Movement
Eph receptor tyrosine kinase
ephrin signaling
Ephrins - metabolism
Humans
Ligands
Mice
MMP
Peptide Hydrolases - metabolism
protease
Protein Binding
Receptors, Eph Family - metabolism
Signal Transduction
Special Focus: Ephrin Signaling: Reviews
γ-secretase
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Proteases regulate a myriad of cell functions, both in normal and disease states. In addition to protein turnover, they regulate a range of signaling processes, including those mediated by Eph receptors and their ephrin ligands. A variety of proteases is reported to directly cleave Ephs and/or ephrins under different conditions, to promote receptor and/or ligand shedding, and regulate receptor/ligand internalisation and signaling. They also cleave other adhesion proteins in response to Eph-ephrin interactions, to indirectly facilitate Eph-mediated functions. Proteases thus contribute to Eph/ephrin mediated changes in cell-cell and cell-matrix interactions, in cell morphology and in cell migration and invasion, in a manner which appears to be tightly regulated by, and co-ordinated with, Eph signaling. This review summarizes the current literature describing the function and regulation of protease activities during Eph/ephrin-mediated cell signaling.
ISSN:1933-6918
1933-6926
DOI:10.4161/19336918.2014.970026