Protein tyrosine phosphatases (PTPs) perform specific functions in vivo, despite being vastly outnumbered by their substrates. Because of this and due to the central roles PTPs play in regulating cellular function, PTP activity is regulated by a large variety of molecular mechanisms. We review evidence that indicates that the divergent C-terminal tail sequences (C-terminal domains, CTDs) of receptor-type PTPs (RPTPs) help regulate RPTP function by controlling intermolecular associations in a way that is itself subject to physiological regulation. We propose that the CTD of each RPTP defines an ‘interaction code’ that helps determine molecules it will interact with under various physiological conditions, thus helping to regulate and diversify PTP function.
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Alternative splicing of intrinsically disordered segments can rewire protein interaction networks. In this issue, the Biochemical Society’s Colworth Medal winner, M. Madan Babu explores the contribution of intrinsically disordered regions to protein function, cellular complexity and human disease; see pages 1185–1200. [Credit: Guilhem Chalancon, MRC Laboratory of Molecular Biology, Cambridge, UK.]
Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains Available to Purchase
Maayan Barnea, Tsviya Olender, Mark T. Bedford, Ari Elson; Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains. Biochem Soc Trans 15 October 2016; 44 (5): 1295–1303. doi: https://doi.org/10.1042/BST20160141
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