Abstract
Receptor protein tyrosine phosphatases (RPTPs) form a group of over 20 enzymes in vertebrates, each with unique ectodomains subject to potential extracellular interactions with ligands. It has recently become clear that a remarkably diverse range of ligands exist, including homophilic binders, adhesion molecules, neurotrophin receptors, and proteoglycans. Individual RPTPs can bind several ligands, and vice versa, suggesting that complex cell signaling networks exist. The identification of RPTP ligands and where they are located in tissues remains a challenge for a large number of these enzymes. Here we describe some powerful methods that have proved successful for several research groups, leading to our improved understanding of RPTP-ligand interactions and functional regulation.
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Acknowledgements
Our work addressing RPTP ligands over the past 15 years has been generously funded by the European Commission (HPRN-CT-2000-00085), the Wellcome Trust (Studentship for John Chilton and grant 071418), the Karim Rida Said Foundation (Studentship for F. Haj), University College London Graduate Research Scholarship (Alexandru Aricescu), and the Child Health Research Appeal Trust. We thank Radu Aricescu for helpful advice and we acknowledge Charlotte Coles for the generation of the TrkC-CFP vector used in Fig. 2d.
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Stoker, A.W. (2016). Detection and Identification of Ligands for Mammalian RPTP Extracellular Domains. In: Pulido, R. (eds) Protein Tyrosine Phosphatases. Methods in Molecular Biology, vol 1447. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-3746-2_15
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DOI: https://doi.org/10.1007/978-1-4939-3746-2_15
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