title: PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease.
abstract: Protein tyrosine phosphatases (PTPs) constitute a family of key homeostatic regulators, with wide implications on physiology and disease. Recent findings have unveiled that the biological activity of PTPs goes beyond the dephosphorylation of phospho-proteins to shut down protein tyrosine kinase-driven signaling cascades. Substrates dephosphorylated by clinically relevant PTPs extend to phospholipids and phosphorylated carbohydrates as well. In addition, non-catalytic functions are also used by PTPs to regulate essential cellular functions. Consequently, PTPs have emerged as novel potential therapeutic targets for human diseases, including cancer predispositions, myopathies and neuropathies. In this review, we highlight recent advances on the multifaceted role of lipid-phosphatase PTPs in human pathology, with an emphasis on hereditary diseases. The involved PTP regulatory networks and PTP modulatory strategies with potential therapeutic application are discussed.
authors.forename: Rafael
authors.initials: R
authors.lastname: Pulido
authors.forename: Andrew W
authors.initials: AW
authors.lastname: Stoker
authors.forename: Wiljan J A J
authors.initials: WJ
authors.lastname: Hendriks
mesh_terms: D000595:Amino Acid Sequence; D006801:Humans; D008969:Molecular Sequence Data; D009135:Muscular Diseases / Q000201:enzymology*; D009369:Neoplasms / Q000188:drug therapy / Q000201:enzymology* / Q000235:genetics / Q000473:pathology; D009422:Nervous System Diseases / Q000201:enzymology*; D010743:Phospholipids / Q000378:metabolism; D010766:Phosphorylation; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D010743:Phospholipids; D017027:Protein Tyrosine Phosphatases