Protein tyrosine phosphatases and signalling.
A cornerstone of many cell-signalling events rests on reversible phosphorylation of tyrosine residues on proteins. The reversibility relies on the coordinated actions of protein tyrosine kinases and protein tyrosine phosphatases (PTPs), both of which exist as large protein families. This review focuses on the rapidly evolving field of the PTPs. We now know that rather than simply scavenging phosphotyrosine, the PTPs specifically regulate a wide range of signalling pathways. To illustrate this and to highlight current areas of agreement and contention in the field, this review will present our understanding of PTP action in selected areas and will present current knowledge surrounding the regulatory mechanisms that control PTP enzymes themselves. It will be seen that PTPs control diverse processes such as focal adhesion dynamics, cell-cell adhesion and insulin signalling, and their own actions are in turn regulated by dimerisation, phosphorylation and reversible oxidation.
Stoker
Andrew W
AW
Institute of Child Health, University College London, 30 Guilford Street, London WC1N 1EH, UK. astoker@ich.ucl.ac.uk
D002448:Cell Adhesion; D002468:Cell Physiological Phenomena; D019281:Dimerization; D006801:Humans; D007328:Insulin / Q000378:metabolism; D008024:Ligands; D010084:Oxidation-Reduction; D017027:Protein Tyrosine Phosphatases / Q000378:metabolism*; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D015398:Signal Transduction / Q000502:physiology*
D007328:Insulin; D008024:Ligands; D011505:Protein-Tyrosine Kinases; D017027:Protein Tyrosine Phosphatases