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References from The protein tyrosine phosphatase interactome: beyond catalytic activity. Local targets link to admitted publications; unresolved targets remain external evidence.
SHP2 regulates GluA2 tyrosine phosphorylation required for AMPA receptor endocytosis and mGluR-LTD
10.1073/pnas.2316819121 · 2024 · External reference
SHP2: a pleiotropic target at the interface of cancer and its microenvironment
10.1158/2159-8290.cd-23-0383 · 2023 · External reference
PTEN–PDZ domain interactions: binding of PTEN to PDZ domains of PTPN13
10.1016/j.ymeth.2014.10.017 · 2015 · External reference
Targeting protein phosphatases in cancer immunotherapy and autoimmune disorders
10.1038/s41573-022-00618-w · 2023 · External reference
Protein tyrosine phosphatases in cell adhesion
10.1042/bcj20200511 · 2021 · External reference
Protein tyrosine phosphatases: a new paradigm in an old signaling system?
10.1016/bs.acr.2021.06.001 · 2021 · External reference
Interactomes – scaffolds of cellular systems
10.1016/b978-0-12-394447-4.40037-4 · 2016 · External reference
Protein tyrosine phosphatases: structure, function, and implication in human disease
10.1007/978-1-62703-562-0_13 · 2013 · External reference
Apoptotic signalling targets the post-endocytic sorting machinery of the death receptor Fas/CD95
10.1038/s41467-019-11025-y · 2019 · External reference
Time-resolved phosphoproteomics reveals scaffolding and catalysis-responsive patterns of SHP2-dependent signaling
10.7554/elife.64251 · 2021 · External reference
The receptor protein tyrosine phosphatase PTPRK promotes intestinal repair and catalysis-independent tumour suppression
10.1242/jcs.261914 · 2024 · External reference
Signalosomes as therapeutic targets
10.1016/j.ppedcard.2007.11.012 · 2008 · External reference
Structural dynamics of the human COP9 signalosome revealed by cross-linking mass spectrometry and integrative modeling
10.1073/pnas.1915542117 · 2020 · External reference
Comprehensive interactome mapping of the DNA repair scaffold SLX4 using proximity labeling and affinity purification
10.1021/acs.jproteome.2c00706 · 2023 · External reference
Phenotypic and interaction profiling of the human phosphatases identifies diverse mitotic regulators
10.1016/j.celrep.2016.10.078 · 2016 · External reference
Proximity-labeling proteomics reveals remodeled interactomes and altered localization of pathogenic SHP2 variants
10.1038/s44319-025-00674-4 · 2026 · External reference
Protein-protein interaction networks (PPI) and complex diseases
2014 · External reference
Protein tyrosine phosphatase SHP2/PTPN11 mistargeting as a consequence of SH2-domain point mutations associated with Noonan Syndrome and leukemia
10.1016/j.jprot.2013.04.005 · 2013 · External reference
Mapping protein–protein interactions by mass spectrometry
10.1002/mas.21887 · 2026 · External reference
Using the yeast two-hybrid system to identify interacting proteins
2004 · External reference
A global analysis of the receptor tyrosine kinase-protein phosphatase interactome
10.1016/j.molcel.2016.12.004 · 2017 · External reference
BioID: a screen for protein-protein interactions
10.1002/cpps.51 · 2018 · External reference
Efficient proximity labeling in living cells and organisms with TurboID
10.1038/nbt.4201 · 2018 · External reference
PTPN23-dependent ESCRT machinery functions as a cell death checkpoint
10.1038/s41467-024-54749-2 · 2024 · External reference
The endosomal sorting adaptor HD-PTP is required for ephrin-B:EphB signalling in cellular collapse and spinal motor axon guidance
10.1038/s41598-019-48421-9 · 2019 · External reference
The homophilic receptor PTPRK selectively dephosphorylates multiple junctional regulators to promote cell–cell adhesion
10.7554/elife.44597 · 2019 · External reference
Recent advances in proximity labeling for chemical proteomics: paving the way for in vivo applications
10.1016/j.cbpa.2025.102620 · 2025 · External reference
Microenvironment mapping via Dexter energy transfer on immune cells
10.1126/science.aay4106 · 2020 · External reference
Substrate-trapping techniques in the identification of cellular PTP targets
10.1016/j.ymeth.2004.07.007 · 2005 · External reference
Coupling substrate-trapping with proximity-labeling to identify protein tyrosine phosphatase PTP1B signaling networks
10.1016/j.jbc.2023.104582 · 2023 · External reference
Teaching an old dog new tricks: a new tool for protein tyrosine phosphatase substrate discovery
10.1016/j.jbc.2023.104731 · 2023 · External reference
Accurate structure prediction of biomolecular interactions with AlphaFold 3
10.1038/s41586-024-07487-w · 2024 · External reference
AlphaFold3: an overview of applications and performance insights
10.3390/ijms26083671 · 2025 · External reference
Structure-based kinetic models of modular signaling protein function: focus on Shp2
10.1529/biophysj.106.093484 · 2007 · External reference
The human DEPhOsphorylation database DEPOD: 2019 update
2019 · External reference
The STRING database in 2023: protein–protein association networks and functional enrichment analyses for any sequenced genome of interest
10.1093/nar/gkac1000 · 2023 · External reference
The BioGRID database: a comprehensive biomedical resource of curated protein, genetic, and chemical interactions
10.1002/pro.3978 · 2021 · External reference
Regulation and activity of the phosphatase SHP2: SH2 domains, dephosphorylation activity, and beyond
10.1042/bst20253102 · 2026 · External reference
Deletion of PDK1 caused cardiac malmorphogenesis and heart defects due to profound protein phosphorylation changes mediated by SHP2
10.1007/s12265-023-10380-y · 2023 · External reference
Targeting SHP2 phosphatase in hematological malignancies
10.1080/14728222.2022.2066518 · 2022 · External reference
Effects of a leukemia-associated gain-of-function mutation of SHP-2 phosphatase on interleukin-3 signaling
10.1074/jbc.m507622200 · 2006 · External reference
HD-PTP is a catalytically inactive tyrosine phosphatase due to a conserved divergence in its phosphatase domain
10.1371/journal.pone.0005105 · 2009 · External reference
The open architecture of HD-PTP phosphatase provides new insights into the mechanism of regulation of ESCRT function
10.1038/s41598-017-09467-9 · 2017 · External reference
Dissecting the role of His domain protein tyrosine phosphatase/PTPN23 and ESCRTs in sorting activated epidermal growth factor receptor to the multivesicular body
10.1042/bst20170443 · 2018 · External reference
Recruitment of UBPY and ESCRT exchange drive HD-PTP-dependent sorting of EGFR to the MVB
10.1016/j.cub.2013.02.033 · 2013 · External reference
Haploinsufficiency of the ESCRT component HD-PTP predisposes to cancer
10.1016/j.celrep.2016.04.076 · 2016 · External reference
Endofin is required for HD-PTP and ESCRT-0 interdependent endosomal sorting of ubiquitinated transmembrane cargoes
10.1016/j.isci.2021.103274 · 2021 · External reference
A non-canonical ESCRT pathway, including histidine domain phosphotyrosine phosphatase (HD-PTP), is used for down-regulation of virally ubiquitinated MHC class I
10.1042/bj20150336 · 2015 · External reference
ESCRT-I and PTPN23 mediate microautophagy of ubiquitylated tau aggregates
10.1083/jcb.202406120 · 2025 · External reference
PTPL1: a large phosphatase with a split personality
10.1007/s10555-008-9114-2 · 2008 · External reference
Protein tyrosine phosphatase-N13 promotes myofibroblast resistance to apoptosis in idiopathic pulmonary fibrosis
10.1164/rccm.201707-1497oc · 2018 · External reference
The binding affinity of PTPN13’s tandem PDZ2/3 domain is allosterically modulated
10.1186/s12860-019-0203-6 · 2019 · External reference
The Adenomatous Polyposis Coli-protein (APC) interacts with the protein tyrosine phosphatase PTP-BL via an alternatively spliced PDZ domain
10.1038/sj.onc.1203725 · 2000 · External reference
PTPN13 regulates cellular signalling and β-catenin function during megakaryocytic differentiation
10.1016/j.bbamcr.2014.08.014 · 2014 · External reference
The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif
10.1016/s0014-5793(01)02401-2 · 2001 · External reference
Molecular basis of class III ligand recognition by PDZ3 in murine protein tyrosine phosphatase PTPN13
10.1016/j.jmb.2018.08.023 · 2018 · External reference
Receptor protein-tyrosine phosphatase RPTPμ binds to and dephosphorylates the catenin p120ctn
10.1074/jbc.275.15.11264 · 2000 · External reference
The PTPμ protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts
10.1074/jbc.m010823200 · 2001 · External reference
Expression of the receptor protein-tyrosine phosphatase, PTPμ, restores E-cadherin-dependent adhesion in human prostate carcinoma cells
10.1074/jbc.m112157200 · 2002 · External reference
The receptor protein-tyrosine phosphatase PTPμ interacts with IQGAP1
10.1074/jbc.m506414200 · 2006 · External reference
Association of connexin43 with a receptor protein tyrosine phosphatase
10.1080/cac.10.4-6.201.205 · 2003 · External reference
Involvement of nectin in inactivation of integrin αvβ3 after the establishment of cell-cell adhesion
10.1074/jbc.m704195200 · 2008 · External reference
Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration
10.1002/jcb.22710 · 2011 · External reference
Receptor tyrosine phosphatase R-PTP-κ mediates homophilic binding
1994 · External reference
Determinants of receptor tyrosine phosphatase homophilic adhesion: structural comparison of PTPRK and PTPRM extracellular domains
10.1016/j.jbc.2022.102750 · 2023 · External reference
Molecular mechanism of Afadin substrate recruitment to the receptor phosphatase PTPRK via its pseudophosphatase domain
10.7554/elife.79855 · 2022 · External reference
The tumor suppressor PTPRK promotes ZNRF3 internalization and is required for Wnt inhibition in the Spemann organizer
10.7554/elife.51248 · 2020 · External reference
PTPRK regulates glycolysis and de novo lipogenesis to promote hepatocyte metabolic reprogramming in obesity
10.1038/s41467-024-53733-0 · 2024 · External reference
Elevated protein tyrosine phosphatase kappa expression is associated with disease progression and poor prognosis of pancreatic cancer
10.21873/cdp.10560 · 2026 · External reference
Recent advances in the development of allosteric protein tyrosine phosphatase inhibitors for drug discovery
10.1002/med.21871 · 2022 · External reference
SHP2-targeted cancer therapeutics: structural insights, inhibitor development and emerging modalities
10.1016/j.bmc.2026.118708 · 2026 · External reference
Novel and emerging therapeutic drug targets for management of type 2 Diabetes Mellitus
2021 · External reference
Targeting tyrosine phosphatases: time to end the stigma
10.1016/j.tips.2017.03.004 · 2017 · External reference
Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway
10.1038/s41598-025-20770-8 · 2025 · External reference
Abstract CT073: a first-in-human study of oral TNO155 (batoprotafib) alone and in combination with EGF816 (nazartinib) in adult patients with advanced solid tumors
10.1158/1538-7445.am2025-ct073 · 2025 · External reference
PTPN23 ubiquitination by WDR4 suppresses EGFR and c-MET degradation to define a lung cancer therapeutic target
10.1038/s41419-023-06201-4 · 2023 · External reference
Targeting PTPN13 with 11-amino-acid peptides of C-terminal APC prevents immune evasion of colorectal cancer
10.1038/s41422-025-01206-4 · 2026 · External reference
Proteolytic cleavage of protein tyrosine phosphatase μ regulates glioblastoma cell migration
10.1158/0008-5472.can-09-0863 · 2009 · External reference
A PTPmu biomarker is associated with increased survival in gliomas
10.3390/ijms20102372 · 2019 · External reference
Small molecule antagonists of PTPmu identified by artificial intelligence-based computational screening block glioma cell migration and growth
10.1371/journal.pone.0288980 · 2023 · External reference
