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PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease

Pulido, R; Stoker, AW; Hendriks, WJ; (2013) PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease. Human Molecular Genetics , 22 (R1) R66 - R76. 10.1093/hmg/ddt347. Green open access

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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.

Type: Article
Title: PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.1093/hmg/ddt347
Publisher version: http://dx.doi.org/10.1093/hmg/ddt347
Language: English
Additional information: This is a pre-copyedited, author-produced PDF of an article accepted for publication in [Human Molecular Genetics following peer review. The version of record [Rafael Pulido, Andrew W. Stoker, and Wiljan J.A.J. Hendriks PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease Hum. Mol. Genet. (2013) 22 (R1): R66-R76 first published online July 29, 2013 doi:10.1093/hmg/ddt347 is available online at: http://dx.doi.org/10.1093/hmg/ddt347
Keywords: Amino Acid Sequence, Humans, Molecular Sequence Data, Muscular Diseases, Neoplasms, Nervous System Diseases, Phospholipids, Phosphorylation, Protein Tyrosine Phosphatases, Sequence Alignment, Signal Transduction, Substrate Specificity
UCL classification: UCL
UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Population Health Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Population Health Sciences > UCL GOS Institute of Child Health
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Population Health Sciences > UCL GOS Institute of Child Health > Developmental Biology and Cancer Dept
URI: https://discovery.ucl.ac.uk/id/eprint/1434136
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