Protein Tyrosine Phosphatases

This study identifies PTPRK's role in promoting hepatocyte metabolic reprogramming in obesity by regulating glycolysis and lipogenesis, with potential therapeutic implications for obesity-related liver diseases.

The paper investigates how tyrosine phosphorylation affects PTP-PEST's structure and function by identifying specific phosphorylation sites and their impact on substrate binding and catalytic conformation.

The paper identifies conserved mechanisms by which PP2A-B55 substrates bind B55 through α-helices and develops a competitive inhibitor to study its function.

This study uses an ABA-induced proximity system to reversibly control kinase signaling by recruiting phosphatases, revealing how phosphatases regulate oncogenic kinases like BCR::ABL1, BRAF(V600E), and MEK1.

This study identifies novel functions of the conserved phosphatase PTPN-22 in C. elegans, showing its role in molting, cell adhesion, and cytoskeletal regulation through genetic and proteomic analyses.

This study shows that Shoc2 variants associated with NSLH alter ERK1/2 phosphorylation levels depending on AKT pathway activation, revealing a feedback mechanism in EGFR signaling.

This study identifies CTDNEP1-NEP1R1 as a conserved membrane phosphatase complex that restricts ER expansion, with NEP1R1 activating CTDNEP1 through structural stabilization and substrate orientation.

This study identifies phosphoproteomic targets of protein phosphatases in EGFR signaling using chemical inhibitors and mass spectrometry.

The paper identifies 2,204 potential PPP2CA substrates using proteolysis-targeting chimeras and phospho-proteomic analysis, revealing novel substrates and a pSP/pTP motif preference.

This study shows that loss of Shp1 in zebrafish leads to myeloid cell dysfunction, inflammation, and larval lethality.

The paper identifies how Afadin is recruited to PTPRK via its pseudophosphatase domain, revealing that substrate specificity is determined by interactions outside the active site.

This study identifies an inflammatory response in HSPCs with SHP2 mutations that drives MPN and suggests anti-inflammatory agents as potential therapies for JMML.

The paper identifies the molecular mechanism by which Phactr1/PP1 phosphatase achieves substrate specificity through structural and phosphoproteomic analysis.

CoralP provides an interactive web tool for visualizing human phosphatome data with customizable attributes, offering a unique resource for phosphatase analysis.

The paper curates and scores gene-disease associations for 19 genes related to RASopathies using the ClinGen framework, classifying their associations as definitive, strong, moderate, limited, disputed, or no evidence.

The paper identifies how EGFR interacts with PTPs on juxtaposed membranes to create a network that senses and responds to growth factor signals.

In suspended human keratinocytes, five induced phosphatases dampen ERK to drive differentiation commitment, opposed by DUSP10, in a time-rewired network that renders commitment an unstable switch.