Protein tyrosine phosphatases as adhesion receptors

Brady-Kalnay, S. M., Tonks, N. K. (October 1995) Protein tyrosine phosphatases as adhesion receptors. Current Opinion in Cell Biology, 7 (5). pp. 650-657. ISSN 0955-0674

URL: http://www.ncbi.nlm.nih.gov/pubmed/8573339
DOI: 10.1016/0955-0674(95)80106-5

Abstract

The intracellular segments of classic adhesion molecules such as N-CAM do not show structural similarity to any known signaling molecules. This suggests that their effects on signaling responses must be exerted indirectly through associated proteins. In contrast, many receptor protein tyrosine phosphatases (RPTPs) possess extracellular segments with 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 modulation of catalytic function through engagement of the extracellular segment, 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 homophilic binding or indirectly by association with known cell adhesion molecules. In addition, RPTPs have been localized to points of cell-cell or cell-matrix contact, indicating their potential to regulate these structures.

Item Type: Paper
Uncontrolled Keywords: NEURONAL RECOGNITION MOLECULE CELL-CELL-ADHESION EXTRACELLULAR REGION HOMOPHILIC BINDING PHOSPHORYLATION FIBROBLASTS FAMILY MEMBER GROWTH
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein receptor
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: October 1995
Date Deposited: 18 Dec 2013 15:08
Last Modified: 18 Dec 2013 15:08
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29059

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