PROTEIN-TYROSINE PHOSPHATASES AS ADHESION RECEPTORS

The intracellular segments of classic adhesion molecules such as N-CAM do not show structural similarity to any known signaling molecules. T his suggests that their effects on signaling responses must be exerted indirectly through associated proteins. In contrast, many receptor pr otein tyrosine phosphatases (RPTPs) possess extracellular segments wit h homology to cell adhesion molecules linked directly to intracellular segments comprising one or two protein tyrosine phosphatase catalytic domains. Therefore, the RPTPs have the potential for direct modulatio n of catalytic function through engagement of the extracellular segmen t, suggesting they could be direct signal transducers of cell contact phenomena. in the past few years, some RPTPs have been shown to effect cell-cell adhesion directly via hemophilic binding or indirectly by a ssociation with known cell adhesion molecules. In addition, RPTPs have been localized to points of cell-cell or cell-matrix contact, indicat ing their potential to regulate these structures.