title: Regulation of receptor-type protein tyrosine phosphatases by their C-terminal tail domains.
abstract: 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.
authors.affiliation: Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Maayan
authors.initials: M
authors.lastname: Barnea
authors.affiliation: Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Tsviya
authors.initials: T
authors.lastname: Olender
authors.affiliation: Department of Epigenetics and Molecular Carcinogenesis, MD Anderson Cancer Center, University of Texas, Smithville, TX 78957, USA.
authors.forename: Mark T
authors.initials: MT
authors.lastname: Bedford
authors.affiliation: Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.
authors.forename: Ari
authors.initials: A
authors.lastname: Elson
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D006801:Humans; D008954:Models, Biological; D010766:Phosphorylation; D011485:Protein Binding; D054557:Receptor-Like Protein Tyrosine Phosphatases / Q000737:chemistry / Q000378:metabolism*; D014443:Tyrosine / Q000737:chemistry / Q000378:metabolism*
chemical_list: D014443:Tyrosine; D054557:Receptor-Like Protein Tyrosine Phosphatases
keywords: SH2 domain; phosphorylation/dephosphorylation; protein tyrosine phosphatases; sequence motif