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Статті в журналах з теми "PTPN14"

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Автор: Grafiati

Опубліковано: 10 грудня 2022

Оновлено: 28 січня 2023

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1

Hatterschide, Joshua, Amelia E. Bohidar, Miranda Grace, Tara J. Nulton, Hee Won Kim, Brad Windle, Iain M. Morgan, Karl Munger, and Elizabeth A. White. "PTPN14 degradation by high-risk human papillomavirus E7 limits keratinocyte differentiation and contributes to HPV-mediated oncogenesis." Proceedings of the National Academy of Sciences 116, no. 14 (March 20, 2019): 7033–42. http://dx.doi.org/10.1073/pnas.1819534116.

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High-risk human papillomavirus (HPV) E7 proteins enable oncogenic transformation of HPV-infected cells by inactivating host cellular proteins. High-risk but not low-risk HPV E7 target PTPN14 for proteolytic degradation, suggesting that PTPN14 degradation may be related to their oncogenic activity. HPV infects human keratinocytes but the role of PTPN14 in keratinocytes and the consequences of PTPN14 degradation are unknown. Using an HPV16 E7 variant that can inactivate retinoblastoma tumor suppressor (RB1) but cannot degrade PTPN14, we found that high-risk HPV E7-mediated PTPN14 degradation impairs keratinocyte differentiation. Deletion ofPTPN14from primary human keratinocytes decreased keratinocyte differentiation gene expression. Related to oncogenic transformation, both HPV16 E7-mediated PTPN14 degradation andPTPN14deletion promoted keratinocyte survival following detachment from a substrate. PTPN14 degradation contributed to high-risk HPV E6/E7-mediated immortalization of primary keratinocytes and HPV+but not HPV−cancers exhibit a gene-expression signature consistent with PTPN14 inactivation. We find that PTPN14 degradation impairs keratinocyte differentiation and propose that this contributes to high-risk HPV E7-mediated oncogenic activity independent of RB1 inactivation.

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2

Po’uha, Sela T., Marion Le Grand, Miriam B. Brandl, Andrew J. Gifford, Gregory J. Goodall, Yeesim Khew-Goodall, and Maria Kavallaris. "Stathmin levels alter PTPN14 expression and impact neuroblastoma cell migration." British Journal of Cancer 122, no. 3 (December 6, 2019): 434–44. http://dx.doi.org/10.1038/s41416-019-0669-1.

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Abstract Background Stathmin mediates cell migration and invasion in vitro, and metastasis in vivo. To investigate stathmin’s role on the metastatic process, we performed integrated mRNA–miRNA expression analysis to identify pathways regulated by stathmin. Methods MiRNA and gene arrays followed by miRNA-target-gene integration were performed on stathmin-depleted neuroblastoma cells (CtrlshRNA vs. Stmn Seq2shRNA). The expression of the predicted target PTPN14 was evaluated by RT-qPCR, western blot and immunohistochemistry. Gene-silencing technology was used to assess the role of PTPN14 on proliferation, migration, invasion and signalling pathway. Results Stathmin levels modulated the expression of genes and miRNA in neuroblastoma cells, leading to a deregulation of migration and invasion pathways. Consistent with gene array data, PTPN14 mRNA and protein expression were downregulated in stathmin- depleted neuroblastoma cells and xenografts. In two independent neuroblastoma cells, suppression of PTPN14 expression led to an increase in cell migration and invasion. PTPN14 and stathmin expression did not act in a feedback regulatory loop in PTPN14- depleted cells, suggesting a complex interplay of signalling pathways. The effect of PTPN14 on YAP pathway activation was cell-type dependent. Conclusions Our findings demonstrate that stathmin levels can regulate PTPN14 expression, which can modulate neuroblastoma cell migration and invasion.

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3

LEHRER, STEVEN, and PETER H. RHEINSTEIN. "PTPN14 Mutations and Cervical Cancer." Cancer Diagnosis & Prognosis 1, no. 4 (September 3, 2021): 275–77. http://dx.doi.org/10.21873/cdp.10035.

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Background/Aim: It was recently shown that rare germline loss-of-function variants in the tyrosine-protein phosphatase non-receptor type 14 (PTPN14) gene conferred substantial risk of basal cell carcinoma (BCC). A follow-up investigation of 24 cancers and three benign tumor types showed that PTPN14 loss-of-function variants were associated with high risk of cervical cancer and early age at diagnosis. We used the Cancer Genome Atlas (TCGA) to further evaluate the PTPN14 – cervical cancer association. Materials and Methods: We analyzed the Genomic Data Commons (GDC) TCGA Cervical Cancer (CESC) data set. We used cBioPortal for Cancer Genomics to access data in TCGA. cBioPortal provides visualization, analysis and download options for large-scale cancer genomic data sets. We also accessed TCGA data with the University of California Santa Cruz (UCSC) Xena Browser. UCSC Xena allows users to explore functional genomic data sets for assessing correlations between genomic and/or phenotypic variables. Results: Ten patients with PTPN14 mutations had significantly better survival than 266 patients without PTPN14 mutations (p=0.05 log rank test). In the Human Protein Atlas, low expression of PTPN14 in 85 TCGA cervical cancer specimens was associated with better survival than high expression in 206 cervical cancer specimens. Conclusion: In general, factors that affect the risk of a cancer have the same effect on prognosis. For example, history of allergy reduces risk of malignant brain tumors and improves prognosis. However, this relationship is not the case for PTPN14. We conclude that in TCGA cervical cancer specimens, PTPN14 mutation is a favorable prognostic factor. However, germline variants of PTPN14 confer a worse prognosis. Further studies of the specific mutations would be worthwhile.

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4

Bottini, Angel, Dennis J. Wu, Rizi Ai, Michelle Le Roux, Beatrix Bartok, Michele Bombardieri, Karen M. Doody та ін. "PTPN14 phosphatase and YAP promote TGFβ signalling in rheumatoid synoviocytes". Annals of the Rheumatic Diseases 78, № 5 (26 лютого 2019): 600–609. http://dx.doi.org/10.1136/annrheumdis-2018-213799.

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ObjectiveWe aimed to understand the role of the tyrosine phosphatase PTPN14—which in cancer cells modulates the Hippo pathway by retaining YAP in the cytosol—in fibroblast-like synoviocytes (FLS) from patients with rheumatoid arthritis (RA).MethodsGene/protein expression levels were measured by quantitative PCR and/or Western blotting. Gene knockdown in RA FLS was achieved using antisense oligonucleotides. The interaction between PTPN14 and YAP was assessed by immunoprecipitation. The cellular localisation of YAP and SMAD3 was examined via immunofluorescence. SMAD reporter studies were carried out in HEK293T cells. The RA FLS/cartilage coimplantation and passive K/BxN models were used to examine the role of YAP in arthritis.ResultsRA FLS displayed overexpression of PTPN14 when compared with FLS from patients with osteoarthritis (OA). PTPN14 knockdown in RA FLS impaired TGFβ-dependent expression of MMP13 and potentiation of TNF signalling. In RA FLS, PTPN14 formed a complex with YAP. Expression of PTPN14 or nuclear YAP—but not of a non-YAP-interacting PTPN14 mutant—enhanced SMAD reporter activity. YAP promoted TGFβ-dependent SMAD3 nuclear localisation in RA FLS. Differences in epigenetic marks within Hippo pathway genes, including YAP, were found between RA FLS and OA FLS. Inhibition of YAP reduced RA FLS pathogenic behaviour and ameliorated arthritis severity.ConclusionIn RA FLS, PTPN14 and YAP promote nuclear localisation of SMAD3. YAP enhances a range of RA FLS pathogenic behaviours which, together with epigenetic evidence, points to the Hippo pathway as an important regulator of RA FLS behaviour.

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5

Fu, Panfeng, Ramaswamy Ramchandran, Mark Shaaya, Longshuang Huang, David L. Ebenezer, Ying Jiang, Yulia Komarova, et al. "Phospholipase D2 restores endothelial barrier function by promoting PTPN14-mediated VE-cadherin dephosphorylation." Journal of Biological Chemistry 295, no. 22 (April 23, 2020): 7669–85. http://dx.doi.org/10.1074/jbc.ra119.011801.

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Increased permeability of vascular lung tissues is a hallmark of acute lung injury and is often caused by edemagenic insults resulting in inflammation. Vascular endothelial (VE)-cadherin undergoes internalization in response to inflammatory stimuli and is recycled at cell adhesion junctions during endothelial barrier re-establishment. Here, we hypothesized that phospholipase D (PLD)-generated phosphatidic acid (PA) signaling regulates VE-cadherin recycling and promotes endothelial barrier recovery by dephosphorylating VE-cadherin. Genetic deletion of PLD2 impaired recovery from protease-activated receptor-1–activating peptide (PAR-1–AP)-induced lung vascular permeability and potentiated inflammation in vivo. In human lung microvascular endothelial cells (HLMVECs), inhibition or deletion of PLD2, but not of PLD1, delayed endothelial barrier recovery after thrombin stimulation. Thrombin stimulation of HLMVECs increased co-localization of PLD2-generated PA and VE-cadherin at cell-cell adhesion junctions. Inhibition of PLD2 activity resulted in prolonged phosphorylation of Tyr-658 in VE-cadherin during the recovery phase 3 h post-thrombin challenge. Immunoprecipitation experiments revealed that after HLMVECs are thrombin stimulated, PLD2, VE-cadherin, and protein-tyrosine phosphatase nonreceptor type 14 (PTPN14), a PLD2-dependent protein-tyrosine phosphatase, strongly associate with each other. PTPN14 depletion delayed VE-cadherin dephosphorylation, reannealing of adherens junctions, and barrier function recovery. PLD2 inhibition attenuated PTPN14 activity and reversed PTPN14-dependent VE-cadherin dephosphorylation after thrombin stimulation. Our findings indicate that PLD2 promotes PTPN14-mediated dephosphorylation of VE-cadherin and that redistribution of VE-cadherin at adherens junctions is essential for recovery of endothelial barrier function after an edemagenic insult.

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6

Lu, Yingzhi, Zhenxin Wang, Ling Zhou, Zhaoming Ma, Jianguo Zhang, Yan Wu, Yan Shao, and Yunyun Yang. "FAT1 and PTPN14 Regulate the Malignant Progression and Chemotherapy Resistance of Esophageal Cancer through the Hippo Signaling Pathway." Analytical Cellular Pathology 2021 (October 19, 2021): 1–9. http://dx.doi.org/10.1155/2021/9290372.

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Background. Esophageal cancer (EC) is a common malignant tumor, which brings heavy economic burden to patients and society. Therefore, it is important to understand the molecular mechanism of recurrence, metastasis, and drug resistance of esophageal cancer. Methods. Human esophageal cancer cell line TE13 (poorly differentiated squamous cell carcinoma) and normal human esophageal epithelial cell line het-1a were selected for aseptic culture. At the same time, 6 bottles of TE13 cell line were inoculated in logarithmic phase. Cell apoptosis was analyzed by flow cytometry (FCM). Cell clone formation assay was used to analyze the proliferation. Fibronectin-coated dishes were used to detect the characteristics of cell adhesion to extracellular matrix. The Transwell method was used to detect the cell invasion ability. Western blot was used to analyze the expression of Yap1, PTPN14, FAT1, and Myc. Results. Results showed that FAT1 and PTPN14 were downregulated, while Yap1 was upregulated in esophageal cancer tissues. FAT1 inhibited the proliferation, adhesion, and invasion of human esophageal cancer cell lines, which might be associated with the upregulation of PTPN14 and the inhibition of Yap1 and Myc. Conclusion. The results suggested that PTPN14 and FAT1 could regulate malignant progression and chemotherapy resistance of esophageal cancer based on the Hippo signaling pathway.

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7

Shi, Wenting, and Fang Wang. "circ_AKT3 knockdown suppresses cisplatin resistance in gastric cancer." Open Medicine 17, no. 1 (January 1, 2022): 280–91. http://dx.doi.org/10.1515/med-2021-0355.

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Abstract Background Circular RNAs (circRNAs) are associated with cisplatin resistance in gastric cancer (GC). This study aims to explore the role of circRNA AKT serine/threonine kinase 3 (circ_AKT3) in the resistance of GC to cisplatin. Methods 42 sensitive and 23 resistant GC patients were recruited for tissue collection. The cisplatin-resistant GC cells MKN-7/DDP and HGC-27/DDP were used for in vitro study. circ_AKT3, microRNA-206 (miR-206) and protein tyrosine phosphatase non-receptor type 14 (PTPN14) levels were detected via quantitative reverse transcription real-time PCR (qPCR) and Western blot. Cisplatin resistance was assessed by detecting P-glycoprotein (P-gp) level, half maximal inhibitory concentration (IC50) of cisplatin and cell apoptosis. The target relationship between miR-206 and circ_AKT3 or PTPN14 was analyzed via dual-luciferase reporter and RNA pull-down assays. The role of circ_AKT3 in vivo was assessed using xenograft model. Results circ_AKT3 level was increased, but miR-206 was declined in cisplatin-resistant GC tissues and cells. circ_AKT3 knockdown or miR-206 overexpression decreased the level of P-gp and IC50 of cisplatin and increased apoptosis of MKN-7/DDP and HGC-27/DDP cells. Additionally, circ_AKT3 targeted miR-206, and regulated cisplatin resistance by interacting with miR-206. PTPN14 was regulated by circ_AKT3 through miR-206 as a bridge. Also, circ_AKT3 knockdown decreased xenograft tumor growth. Conclusion circ_AKT3 knockdown suppressed cisplatin resistance using miR-206/PTPN14 axis in cisplatin-resistant GC cells.

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8

Yoon, Sun-Young, Jinsoo Kim, Bum Soo Lee, Su Cheol Baek, Sang J. Chung, and Ki Hyun Kim. "Terminalin from African Mango (Irvingia gabonensis) Stimulates Glucose Uptake through Inhibition of Protein Tyrosine Phosphatases." Biomolecules 12, no. 2 (February 17, 2022): 321. http://dx.doi.org/10.3390/biom12020321.

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Protein tyrosine phosphatases (PTPs), along with protein tyrosine kinases, control signaling pathways involved in cell growth, metabolism, differentiation, proliferation, and survival. Several PTPs, such as PTPN1, PTPN2, PTPN9, PTPN11, PTPRS, and DUSP9, disrupt insulin signaling and trigger type 2 diabetes, indicating that PTPs are promising drug targets for the treatment or prevention of type 2 diabetes. As part of an ongoing study on the discovery of pharmacologically active bioactive natural products, we conducted a phytochemical investigation of African mango (Irvingia gabonensis) using liquid chromatography–mass spectrometry (LC/MS)-based analysis, which led to the isolation of terminalin as a major component from the extract of the seeds of I. gabonensis. The structure of terminalin was characterized by spectroscopic methods, including one-dimensional (1D) and two-dimensional (2D) nuclear magnetic resonance (NMR) and high-resolution (HR) electrospray ionization (ESI) mass spectroscopy. Moreover, terminalin was evaluated for its antidiabetic property; terminalin inhibited the catalytic activity of PTPN1, PTPN9, PTPN11, and PTPRS in vitro and led to a significant increase in glucose uptake in differentiated C2C12 muscle cells, indicating that terminalin exhibits antidiabetic effect through the PTP inhibitory mechanism. These findings suggest that terminalin derived from African mango could be used as a functional food ingredient or pharmaceutical supplement for the prevention of type 2 diabetes.

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9

Choi, Jaewoo, Anita Saraf, Laurence Florens, Michael P. Washburn, and Luca Busino. "PTPN14 regulates Roquin2 stability by tyrosine dephosphorylation." Cell Cycle 17, no. 18 (September 17, 2018): 2243–55. http://dx.doi.org/10.1080/15384101.2018.1522912.

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10

Wang, W., J. Huang, X. Wang, J. Yuan, X. Li, L. Feng, J. I. Park, and J. Chen. "PTPN14 is required for the density-dependent control of YAP1." Genes & Development 26, no. 17 (September 1, 2012): 1959–71. http://dx.doi.org/10.1101/gad.192955.112.

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11

Liu, X., N. Yang, S. A. Figel, K. E. Wilson, C. D. Morrison, I. H. Gelman, and J. Zhang. "PTPN14 interacts with and negatively regulates the oncogenic function of YAP." Oncogene 32, no. 10 (April 23, 2012): 1266–73. http://dx.doi.org/10.1038/onc.2012.147.

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12

Michaloglou, Chrysiis, Waltraut Lehmann, Typhaine Martin, Clara Delaunay, Andreas Hueber, Louise Barys, Honglin Niu, et al. "The Tyrosine Phosphatase PTPN14 Is a Negative Regulator of YAP Activity." PLoS ONE 8, no. 4 (April 16, 2013): e61916. http://dx.doi.org/10.1371/journal.pone.0061916.

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13

Belle, Leila, Naveid Ali, Ana Lonic, Xiaochun Li, James L. Paltridge, Suraya Roslan, David Herrmann, et al. "The tyrosine phosphatase PTPN14 (Pez) inhibits metastasis by altering protein trafficking." Science Signaling 8, no. 364 (February 17, 2015): ra18. http://dx.doi.org/10.1126/scisignal.2005547.

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14

Wang, Chin-Chou, Wan-Jou Shen, Gangga Anuraga, Hoang Dang Khoa Ta, Do Thi Minh Xuan, Sih-Tong Chen, Chiu-Fan Shen, et al. "Novel Potential Therapeutic Targets of PTPN Families for Lung Cancer." Journal of Personalized Medicine 12, no. 12 (November 23, 2022): 1947. http://dx.doi.org/10.3390/jpm12121947.

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Despite the treatment of lung adenocarcinoma (LUAD) having partially improved in recent years, LUAD patients still have poor prognosis rates. Therefore, it is especially important to explore effective biomarkers and exploit novel therapeutic developments. High-throughput technologies are widely used as systematic approaches to explore differences in expressions of thousands of genes for both biological and genomic systems. Recently, using big data analyses in biomedicine research by integrating several high-throughput databases and tools, including The Cancer Genome Atlas (TCGA), cBioportal, Oncomine, and Kaplan–Meier plotter, is an important strategy to identify novel biomarkers for cancer therapy. Here, we used two different comprehensive bioinformatics analysis and revealed protein tyrosine phosphatase non-receptor type (PTPN) family genes, especially PTPN1 and PTPN22, were downregulated in lung cancer tissue in comparison with normal samples. The survival curves indicated that LUAD patients with high transcription levels of PTPN5 were significantly associated with a good prognosis. Meanwhile, Gene Ontology (GO) and MetaCore analyses indicated that co-expression of the PTPN1, PTPN5, and PTPN21 genes was significantly enriched in cancer development-related pathways, including GTPase activity, regulation of small GTPase-mediated signal transduction, response to mechanical stimuli, vasculogenesis, organ morphogenesis, regulation of stress fiber assembly, mitogen-activated protein kinase (MAPK) cascade, cell migration, and angiogenesis. Collectively, this study revealed that PTPN family members are both significant prognostic biomarkers for lung cancer progression and promising clinical therapeutic targets, which provide new targets for treating LUAD patients.

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15

Russell-Goldman, Eleanor, Fei Dong, and John Hanna. "Recurrent PTPN14 Mutations in Trichilemmoma: Evidence for Distinct Pathways of Molecular Pathogenesis." American Journal of Dermatopathology 44, no. 8 (July 2, 2021): 545–52. http://dx.doi.org/10.1097/dad.0000000000002015.

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16

Wilson, Kayla, Nuo Yang, Ashley Mussell, and Jianmin Zhang. "The Regulatory Role of KIBRA and PTPN14 in Hippo Signaling and Beyond." Genes 7, no. 6 (May 27, 2016): 23. http://dx.doi.org/10.3390/genes7060023.

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17

Mamai, Ons. "P189 IDENTIFYING PTPN14-DEPENDENT MECHANISMS THAT INFLUENCE CLINICAL MANIFESTATIONS OF HEREDITARY HEMORRHAGIC TELANGIECTASIA." Artery Research 20, no. C (2017): 108. http://dx.doi.org/10.1016/j.artres.2017.10.190.

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18

Barr, Alastair J., Judit É. Debreczeni, Jeyanthy Eswaran, and Stefan Knapp. "Crystal structure of human protein tyrosine phosphatase 14 (PTPN14) at 1.65-Å resolution." Proteins: Structure, Function, and Bioinformatics 63, no. 4 (March 13, 2006): 1132–36. http://dx.doi.org/10.1002/prot.20958.

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19

Olafsdottir, Thorhildur, Simon N. Stacey, Gardar Sveinbjornsson, Gudmar Thorleifsson, Kristjan Norland, Bardur Sigurgeirsson, Kristin Thorisdottir, et al. "Loss-of-Function Variants in the Tumor-Suppressor Gene PTPN14 Confer Increased Cancer Risk." Cancer Research 81, no. 8 (February 18, 2021): 1954–64. http://dx.doi.org/10.1158/0008-5472.can-20-3065.

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20

Huang, Huimin, Yongtao Li, Dongliang Li, Li Wang, Wenqiang Jiao, Yilin Bai, and Gaiping Zhang. "The tyrosine phosphatase PTPN14 inhibits the activation of STAT3 in PEDV infected Vero cells." Veterinary Microbiology 267 (April 2022): 109391. http://dx.doi.org/10.1016/j.vetmic.2022.109391.

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21

Han, Xiu-juan, Li Xue, Li Gong, Shao-jun Zhu, Li Yao, Shu-mei Wang, Miao Lan, Wei Zhang, and Yan-hong Li. "Stat3 Inhibits PTPN13 Expression in Squamous Cell Lung Carcinoma through Recruitment of HDAC5." BioMed Research International 2013 (2013): 1–7. http://dx.doi.org/10.1155/2013/468963.

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Proteins of the protein tyrosine phosphatase (PTP) family are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, and apoptosis. PTPN13 (also known as FAP1, PTPL1, PTPLE, PTPBAS, and PTP1E), a putative tumor suppressor, is frequently inactivated in lung carcinoma through the loss of either mRNA or protein expression. However, the molecular mechanisms underlying its dysregulation have not been fully explored. Interleukin-6 (IL-6) mediated Stat3 activation is viewed as crucial for multiple tumor growth and progression. Here, we demonstrate that PTPN13 is a direct transcriptional target of Stat3 in the squamous cell lung carcinoma. Our data show that IL-6 administration or transfection of a constitutively activated Stat3 in HCC-1588 and SK-MES-1 cells inhibits PTPN13 mRNA transcription. Using luciferase reporter and ChIP assays, we show that Stat3 binds to the promoter region of PTPN13 and promotes its activity through recruiting HDAC5. Thus, our results suggest a previously unknown Stat3-PTPN13 molecular network controlling squamous cell lung carcinoma development.

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22

Zhangyuan, Guangyan, Yin Yin, Wenjie Zhang, WeiWei Yu, Kangpeng Jin, Fei Wang, Ruyi Huang, Haiyuan Shen, Xiaochen Wang, and Beicheng Sun. "Prognostic Value of Phosphotyrosine Phosphatases in Hepatocellular Carcinoma." Cellular Physiology and Biochemistry 46, no. 6 (2018): 2335–46. http://dx.doi.org/10.1159/000489625.

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Background/Aims: During the occurrence and progression of hepatocellular carcinoma (HCC), phosphotyrosine phosphatases (PTPs) are usually described as tumor suppressors or proto-oncogenes, and to some degree are correlated with the prognosis of HCC. Methods: A total of 321 patients from the Cancer Genome Atlas (TCGA) database and 180 patients from our validated cohort with hepatocellular carcinoma were recruited in this study. Kaplan-Meier, univariate and multivariate Cox proportional hazards model were used to evaluate the risk factors for survival. Quantitative real-time PCR (qRT-PCR) and immunohistochemistry (IHC) were applied to detect the expression levels of PTP genes. Results: After screening the data of TCGA, we identified five PTPs as HCC overall survival related PTP genes, among which only three (PTPN12, PTPRN, PTPN18) exhibited differential expression levels in our 180 paired HCC and adjacent tissues (P< 0.001). Further analysis revealed that expression of PTPN18 was positively, but PTPRN was negatively associated with prognosis of HCC both in TCGA cohort and our own cohort. As to PTPN12, results turned out to be opposite according to HBV status. In detail, higher expression of PTPN12 was associated with better outcome in HBV group but worse prognosis in Non-HBV group. Conclusion: Our results suggested that PTPN12, PTPRN and PTPN18 were independent prognostic factors in HCC.

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23

Wang, Shumin, Mei Ping, Bin Song, Yarong Guo, Yuanfei Li, and Junmei Jia. "Exosomal CircPRRX1 Enhances Doxorubicin Resistance in Gastric Cancer by Regulating MiR-3064-5p/PTPN14 Signaling." Yonsei Medical Journal 61, no. 9 (2020): 750. http://dx.doi.org/10.3349/ymj.2020.61.9.750.

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24

Au, Audrey C., Paolo A. Hernandez, Ernest Lieber, Ali M. Nadroo, Yu-Ming Shen, Kevin A. Kelley, Bruce D. Gelb, and George A. Diaz. "Protein Tyrosine Phosphatase PTPN14 Is a Regulator of Lymphatic Function and Choanal Development in Humans." American Journal of Human Genetics 87, no. 3 (September 2010): 436–44. http://dx.doi.org/10.1016/j.ajhg.2010.08.008.

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25

Karaca Atabay, Elif, Carmen Mecca, Qi Wang, Chiara Ambrogio, Ines Mota, Nina Prokoph, Giulia Mura, et al. "Tyrosine phosphatases regulate resistance to ALK inhibitors in ALK+ anaplastic large cell lymphoma." Blood 139, no. 5 (February 3, 2022): 717–31. http://dx.doi.org/10.1182/blood.2020008136.

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Abstract Anaplastic large cell lymphomas (ALCLs) frequently carry oncogenic fusions involving the anaplastic lymphoma kinase (ALK) gene. Targeting ALK using tyrosine kinase inhibitors (TKIs) is a therapeutic option in cases relapsed after chemotherapy, but TKI resistance may develop. By applying genomic loss-of-function screens, we identified PTPN1 and PTPN2 phosphatases as consistent top hits driving resistance to ALK TKIs in ALK+ ALCL. Loss of either PTPN1 or PTPN2 induced resistance to ALK TKIs in vitro and in vivo. Mechanistically, we demonstrated that PTPN1 and PTPN2 are phosphatases that bind to and regulate ALK phosphorylation and activity. In turn, oncogenic ALK and STAT3 repress PTPN1 transcription. We found that PTPN1 is also a phosphatase for SHP2, a key mediator of oncogenic ALK signaling. Downstream signaling analysis showed that deletion of PTPN1 or PTPN2 induces resistance to crizotinib by hyperactivating SHP2, the MAPK, and JAK/STAT pathways. RNA sequencing of patient samples that developed resistance to ALK TKIs showed downregulation of PTPN1 and PTPN2 associated with upregulation of SHP2 expression. Combination of crizotinib with a SHP2 inhibitor synergistically inhibited the growth of wild-type or PTPN1/PTPN2 knock-out ALCL, where it reverted TKI resistance. Thus, we identified PTPN1 and PTPN2 as ALK phosphatases that control sensitivity to ALK TKIs in ALCL and demonstrated that a combined blockade of SHP2 potentiates the efficacy of ALK inhibition in TKI-sensitive and -resistant ALK+ ALCL.

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26

Lin, Yiyang, Zhulin Shao, Meng Zhao, Jinghui Li, and Xiangjin Xu. "PTPN14 deficiency alleviates podocyte injury through suppressing inflammation and fibrosis by targeting TRIP6 in diabetic nephropathy." Biochemical and Biophysical Research Communications 550 (April 2021): 62–69. http://dx.doi.org/10.1016/j.bbrc.2020.12.030.

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Mello, Stephano S., Liz J. Valente, Nitin Raj, Jose A. Seoane, Brittany M. Flowers, Jacob McClendon, Kathryn T. Bieging-Rolett, et al. "A p53 Super-tumor Suppressor Reveals a Tumor Suppressive p53-Ptpn14-Yap Axis in Pancreatic Cancer." Cancer Cell 32, no. 4 (October 2017): 460–73. http://dx.doi.org/10.1016/j.ccell.2017.09.007.

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Sebastian, E., T. Cui, E. H. Bell, J. McElroy, B. Johnson, P. Gulati, M. Geurts, et al. "Characterization of a Novel mir-4516-PTPN14 Therapeutic Resistance Pathway Induced By Radiation Treatment In Glioblastoma." International Journal of Radiation Oncology*Biology*Physics 108, no. 3 (November 2020): e572. http://dx.doi.org/10.1016/j.ijrobp.2020.07.1761.

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Wilson, Kayla E., Ying-Wei Li, Nuo Yang, He Shen, Ashley R. Orillion, and Jianmin Zhang. "PTPN14 Forms a Complex with Kibra and LATS1 Proteins and Negatively Regulates the YAP Oncogenic Function." Journal of Biological Chemistry 289, no. 34 (July 14, 2014): 23693–700. http://dx.doi.org/10.1074/jbc.m113.534701.

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30

Yang, Yujie, Qiannan Ma, Zhiyu Li, Hui Wang, Chenghu Zhang, Yajin Liu, Bochuan Li, et al. "Harmine alleviates atherogenesis by inhibiting disturbed flow‐mediated endothelial activation via protein tyrosine phosphatase PTPN14 and YAP." British Journal of Pharmacology 178, no. 7 (February 15, 2021): 1524–40. http://dx.doi.org/10.1111/bph.15378.

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Cui, Tiantian, Erica H. Bell, Joseph McElroy, Aline Paixao Becker, Pooja Manchanda Gulati, Marjolein Geurts, Nikol Mladkova, et al. "miR-4516 predicts poor prognosis and functions as a novel oncogene via targeting PTPN14 in human glioblastoma." Oncogene 38, no. 16 (December 17, 2018): 2923–36. http://dx.doi.org/10.1038/s41388-018-0601-9.

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Yun, Hye-Yeoung, Min Wook Kim, Hye Seon Lee, Wantae Kim, Ji Hye Shin, Hyunmin Kim, Ho-Chul Shin, et al. "Structural basis for recognition of the tumor suppressor protein PTPN14 by the oncoprotein E7 of human papillomavirus." PLOS Biology 17, no. 7 (July 19, 2019): e3000367. http://dx.doi.org/10.1371/journal.pbio.3000367.

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Zhu, Yihao, and Yao Zu. "Comprehensive Bioinformatics Analysis Reveals PTPN1 (PTP1B) Is a Promising Immunotherapy Target Associated with T Cell Function for Liver Cancer." Journal of Healthcare Engineering 2023 (January 27, 2023): 1–19. http://dx.doi.org/10.1155/2023/1533794.

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Recently, PTP1B was identified as a novel immune checkpoint whose removal can unleash T cell responses. However, research on the influence of PTP1B as an immune regulator on liver cancer is limited. This study aimed to investigate the immunological correlation and function of PTP1B in liver cancer. The expression profiles and corresponding clinical information of liver cancer patients were obtained from the TCGA and ICGC databases. GSE146115 and GSE98638 retrieved from the GEO database were used for the single-cell RNA-seq analysis. The mRNA expression of PTP1B (PTPN1) was increased in patients with most malignancies (all p < 0.05 ), including liver cancer ( p < 0.001 ). Furthermore, up-regulated PTPN1 was connected to advanced tumor stage ( p < 0.05 ) and worse prognosis ( p < 0.01 ) in liver cancer. Through Cox regression analysis, PTPN1 was considered as an independent prognosis factor of overall survival ( p < 0.05 ) and acted as a high-risk factor (hazard ratio > 1). Gene function and pathway analysis suggested PTPN1 was involved in T cell-related immune responses. Moreover, a close relationship was also found between PTPN1 expression and immune checkpoints as well as immune cells, especially with T cell-related checkpoints (all p < 0.001 ) and T cells (all p < 0.001 ). Single-cell RNA-seq analysis further illustrated that the enrichment of PTPN1 in the T cell population may be linked to its exhaustion in the liver cancer microenvironment. Overall, PTPN1 (PTP1B) closely related to T cell may function as an immunotherapy target for liver cancer.

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Dougall, David, and Nicolai van Oers. "PTPN4 and PTPN3 regulation of ITAM containing proteins (50.9)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 50.9. http://dx.doi.org/10.4049/jimmunol.184.supp.50.9.

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Abstract The T cell receptor (TCR) uses a highly conserved ITAM signaling pathway to transduce intracellular signals following appropriate ligand binding. Activations of the ITAM signaling pathway is tightly controlled by diverse families of protein tyrosine kinases and protein tyrosine phosphatases. In earlier studies, we reported that two PTPases (PTPN3 and PTPN4) could directly dephosphorylate the tyrosine residues in the CD3 z ITAMs. However, T cells from both PTPN3 and PTPN4-deficient mice exhibit normal CD3 regulated ITAM signaling pathways. Since PTPN3 and PTPN4 have FERM domains that localize these enzymes to the cytoskeleton, it is possible that these PTPases target distinct proteins. Interestingly, moesin, ezrin, and dectin-1 are three cytoskeletal associated proteins that use ITAM sequences to transduce intracellular signals. To examine whether these distinct ITAM-containing proteins were dephosphorylated by PTPN3 or PTPN4, a combination of transient transfection assays and cell signaling studies in PTPase-deficient dendritic cells were performed. These experiments will reveal whether this PTPase-family dephosphorylates distinct ITAM-containing proteins.

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35

Wang, Li-Juan, Chen-Chen He, Xin Sui, Meng-Jiao Cai, Cong-Ya Zhou, Jin-Lu Ma, Lei Wu, Hao Wang, Su-Xia Han, and Qing Zhu. "MiR-21 promotes intrahepatic cholangiocarcinoma proliferation and growth in vitro and in vivo by targeting PTPN14 and PTEN." Oncotarget 6, no. 8 (February 28, 2015): 5932–46. http://dx.doi.org/10.18632/oncotarget.3465.

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36

Cogulu, Ozgur, Neda Mojarrab, Ozguc S. Simsir, Asude Durmaz, Ayca Aykut, and Dilsah Cogulu. "Association of mutation in PTPN14 gene and gingival fibromatosis with distinctive facies: a novel finding in whole exome sequencing." Clinical Dysmorphology 30, no. 2 (January 22, 2021): 93–99. http://dx.doi.org/10.1097/mcd.0000000000000363.

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Atabay, Elif, Qi Wang, Ambrogio Chiara, Taek-Chin Cheong, Silvia Peola, Geeta G. Sharma, Luca Mologni, Carlo Gambacorti-Passerini, Claudia Voena, and Roberto Chiarle. "Identifying Novel Mechanisms of Resistance to Tyrosine Kinase Inhibitors in Anaplastic Large Cell Lymphoma." Blood 134, Supplement_1 (November 13, 2019): 5060. http://dx.doi.org/10.1182/blood-2019-132188.

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INTRODUCTION: Anaplastic large cell lymphomas (ALCL) frequently carry oncogenic fusion proteins as a consequence of chromosomal translocations of the anaplastic lymphoma kinase (ALK) gene. The fusion protein resulting from the translocation between dimerization domain of nucleophosmin (NPM) and intracellular tyrosine kinase domain of ALK activates several signaling pathways, promoting cell growth, transformation, migration, and survival of the cells. Chemotherapy has been used as a standard treatment approach for ALCL patients, yet about 30% of patients relapse. A more specific treatment method is based on targeting ALK tyrosine kinase using tyrosine kinase inhibitors (TKIs). Crizotinib is an ALK TKI that is approved for the treatment of ALK-rearranged lung cancer and has received Breakthrough Therapy designation for lymphoma because of its high activity in chemo refractory ALCL. However, as for lung cancer, also ALCL patient develop crizotinib resistance due to ALK mutations or unknown mechanisms. In this study, we aimed at elucidating unknown by-pass mechanisms of crizotinib resistance in ALCL. METHODS: We used Genome-wide CRISPR-Cas9 Knockout Screening (GeCKO) to identify candidate genes that contribute to resistance to crizotinib. Four different ALCL cell lines were infected with Lenti-GeCKO libraries. After treatment with crizotinib for 14 days, DNA isolation and next generation sequencing was performed on crizotinib resistant cells to identify candidate genes depleted by the GeCKO screening. Top candidates were selected for validation assays and further analyses. RESULTS: We identified two phosphatases, PTPN1 and PTPN2, in different ALCL cell lines as consistent top hits. Functional validation of these candidate genes showed that single loss of either PTPN1 or PTPN2 generate immediate resistance to crizotinib in ALCL cell lines. Analysis of downstream pathways showed that while loss of PTPN1 activates primarily the MAPK pathway, loss of PTPN2 promotes persistent STAT3 and MAPK activation in ALK inhibited cells. Remarkably, in PTPN1 knockout cells we observed hyperactivation of SHP2, an oncogenic phosphatase that positively regulates the RAS-MAPK pathway. On the other hand, over-expression of PTPN1 and PTPN2 partially inhibited SHP2 phosphorylation. A treatment that combined crizotinib and the recently developed SHP2 inhibitor completely blocked the sustained ERK phosphorylation and reverted the crizotinib resistance observed in PTPN1 and PTPN2 deficient lymphoma cells. CONCLUSIONS: GeCKO library screen identified PTPN1 and PTPN2 as specific genes that mediate crizotinib resistance in ALCL cell lines. Loss of PTPN1 and PTPN2 drives resistance by activating MAPK and/or JAK-STAT pathway. Combined inhibition of SHP2 is a potent therapeutic approach to overcome resistance to crizotinib in ALCL cells. Disclosures Gambacorti-Passerini: Bristol-Meyers Squibb: Consultancy; Pfizer: Honoraria, Research Funding.

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38

Lucci, Maria Antonietta, Rosaria Orlandi, Tiziana Triulzi, Elda Tagliabue, Andrea Balsari, and Emma Villa-Moruzzi. "Expression Profile of Tyrosine Phosphatases in HER2 Breast Cancer Cells and Tumors." Analytical Cellular Pathology 32, no. 5-6 (January 1, 2010): 361–72. http://dx.doi.org/10.1155/2010/386484.

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Background: HER2-overexpression promotes malignancy by modulating signalling molecules, which include PTPs/DSPs (protein tyrosine and dual-specificity phosphatases). Our aim was to identify PTPs/DSPs displaying HER2-associated expression alterations.Methods: HER2 activity was modulated in MDA-MB-453 cells and PTPs/DSPs expression was analysed with a DNA oligoarray, by RT-PCR and immunoblotting. Two public breast tumor datasets were analysed to identify PTPs/DSPs differentially expressed in HER2-positive tumors.Results: In cells (1) HER2-inhibition up-regulated 4 PTPs (PTPRA, PTPRK, PTPN11, PTPN18) and 11 DSPs (7 MKPs [MAP Kinase Phosphatases], 2 PTP4, 2 MTMRs [Myotubularin related phosphatases]) and down-regulated 7 DSPs (2 MKPs, 2 MTMRs, CDKN3, PTEN, CDC25C); (2) HER2-activation with EGF affected 10 DSPs (5 MKPs, 2 MTMRs, PTP4A1, CDKN3, CDC25B) and PTPN13; 8 DSPs were found in both groups. Furthermore, 7 PTPs/DSPs displayed also altered protein level. Analysis of 2 breast cancer datasets identified 6 differentially expressed DSPs: DUSP6, strongly up-regulated in both datasets; DUSP10 and CDC25B, up-regulated; PTP4A2, CDC14A and MTMR11 down-regulated in one dataset.Conclusions: Several DSPs, mainly MKPs and, unexpectedly, MTMRs, were altered following HER2-modulation in cells and 3 DSPs (DUSP6, CDC25B and MTMR11) were altered in both cells and tumors. Among these, DUSP6, strongly up-regulated in HER2-positive tumors, would deserve further investigation as tumor marker or potential therapy target.

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Lim, Dahwan, Chang Hoon Lee, Ho-Chul Shin, Seung Jun Kim, and Bonsu Ku. "Crystallization and preliminary diffraction analysis of the phosphatase domain of PTPN14 in the human papillomavirus E7 binding-defective mutant form." BIODESIGN 9, no. 4 (December 30, 2021): 63–66. http://dx.doi.org/10.34184/kssb.2021.9.4.63.

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40

Liang, Gaofeng, Chaopeng Duan, June He, Wei Ma, and Xing Dai. "PTPN14, a target gene of miR‐4295, restricts the growth and invasion of osteosarcoma cells through inactivation of YAP1 signalling." Clinical and Experimental Pharmacology and Physiology 47, no. 7 (March 25, 2020): 1301–10. http://dx.doi.org/10.1111/1440-1681.13296.

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41

Szelachowska, J., D. Zielecka-Debska, K. Lichon, A. Pomiecko-Olszowy, A. Maciejczyk, R. Matkowski, and A. Chalon. "EP-1144: PTPN14 as a potential marker of local recurrence after PORT in patients with SCC of the oral cavity." Radiotherapy and Oncology 127 (April 2018): S642—S643. http://dx.doi.org/10.1016/s0167-8140(18)31454-3.

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42

Bordbar, Arash, Reza Maroofian, Pia Ostergaard, Mandana Kashaki, Sara Nikpour, Kristiana Gordon, Andrew Crosby, Pedram Khosravi, and Azadeh Shojaei. "A homozygous loss-of-function mutation in PTPN14 causes a syndrome of bilateral choanal atresia and early infantile-onset lymphedema." Meta Gene 14 (December 2017): 53–58. http://dx.doi.org/10.1016/j.mgene.2017.07.006.

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43

Wu, Chia-Lun, Bree Buszard, Chun-Hung Teng, Wei-Lin Chen, Coral G. Warr, Tony Tiganis, and Tzu-Ching Meng. "Dock/Nck facilitates PTP61F/PTP1B regulation of insulin signalling." Biochemical Journal 439, no. 1 (September 14, 2011): 151–59. http://dx.doi.org/10.1042/bj20110799.

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PTP1B (protein tyrosine phosphatase 1B) is a negative regulator of IR (insulin receptor) activation and glucose homoeostasis, but the precise molecular mechanisms governing PTP1B substrate selectivity and the regulation of insulin signalling remain unclear. In the present study we have taken advantage of Drosophila as a model organism to establish the role of the SH3 (Src homology 3)/SH2 adaptor protein Dock (Dreadlocks) and its mammalian counterpart Nck in IR regulation by PTPs. We demonstrate that the PTP1B orthologue PTP61F dephosphorylates the Drosophila IR in S2 cells in vitro and attenuates IR-induced eye overgrowth in vivo. Our studies indicate that Dock forms a stable complex with PTP61F and that Dock/PTP61F associate with the IR in response to insulin. We report that Dock is required for effective IR dephosphorylation and inactivation by PTP61F in vitro and in vivo. Furthermore, we demonstrate that Nck interacts with PTP1B and that the Nck/PTP1B complex inducibly associates with the IR for the attenuation of IR activation in mammalian cells. Our studies reveal for the first time that the adaptor protein Dock/Nck attenuates insulin signalling by recruiting PTP61F/PTP1B to its substrate, the IR.

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44

Shaw, Ameera M., Ahmad Qasem, and Saleh A. Naser. "Modulation of PTPN2/22 Function by Spermidine in CRISPR-Cas9-Edited T-Cells Associated with Crohn’s Disease and Rheumatoid Arthritis." International Journal of Molecular Sciences 22, no. 16 (August 18, 2021): 8883. http://dx.doi.org/10.3390/ijms22168883.

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Crohn’s Disease (CD) and Rheumatoid Arthritis (RA) share some single nucleotide polymorphisms (SNPs) in protein tyrosine phosphatase non-receptor types 2 and 22 (PTPN2/22). Recently, we reported that clinical samples from CD and RA patients associated with PTPN2:rs478582 or PTPN22:rs2476601 genotypes were linked to overactive immune response and exacerbation of inflammation. Here, we investigated in vitro the effects of these SNPs in Jurkat T-cells using CRISPR-Cas9. All cells were evaluated for PTPN22/22 loss of function and effects on cell response. We measured gene expression via RT-qPCR and cytokines by ELISA. We also measured cell proliferation using a BrdU labeling proliferation ELISA, and T-cell activation using CD-25 fluorescent immunostaining. In PTPN2 SNP-edited cells, PTPN2 expression decreased by 3.2-fold, and proliferation increased by 10.2-fold compared to control. Likewise, expression of PTPN22 decreased by 2.4-fold and proliferation increased by 8.4-fold in PTPN22 SNP-edited cells. IFN-γ and TNF-α secretions increased in both edited cell lines. CD25 expression (cell activation) was 80.32% in PTPN2 SNP-edited cells and 85.82% in PTPN22 SNP-edited cells compared to 70.48% in unedited Jurkat T-cells. Treatment of PTPN2 and PTPN22-edited cells with a maximum 20 μM spermidine restored PTPN2/22 expression and cell response including cell proliferation, activation, and cytokines secretion. Most importantly, the effect of spermidine on edited cells restored normal expression and secretion of IFN-γ and TNF-α. The data clearly demonstrated that edited SNPs in PTPN2 or PTPN22 were associated with reduced gene expression, which resulted in an increase in cell proliferation and activation and overactive immune response. The data validated our earlier observations in CD and RA clinical samples. Surprisingly, spermidine restored PTPN2/22 expression in edited Jurkat T-cells and the consequent beneficial effect on cell response and inflammation. The study supports the use of polyamines dietary supplements for management of CD and in RA patients.

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Wang, Rong, Yonghao Du, Jin Shang, Xiaomin Dang, and Gang Niu. "PTPN14 acts as a candidate tumor suppressor in prostate cancer and inhibits cell proliferation and invasion through modulating LATS1/YAP signaling." Molecular and Cellular Probes 53 (October 2020): 101642. http://dx.doi.org/10.1016/j.mcp.2020.101642.

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46

Cui, T., E. H. Bell, J. McElroy, A. Becker, P. Gulati, M. Geurts, N. Mladkova, et al. "miR-4516 is a Novel Prognostic Biomarker and Promotes Tumorigenesis via Targeting PTPN14-Mediated Regulation of the Hippo Pathway in Glioblastoma." International Journal of Radiation Oncology*Biology*Physics 102, no. 3 (November 2018): e176-e177. http://dx.doi.org/10.1016/j.ijrobp.2018.07.656.

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47

Freiss, Gilles, and Dany Chalbos. "PTPN13/PTPL1: An Important Regulator of Tumor Aggressiveness." Anti-Cancer Agents in Medicinal Chemistry 11, no. 1 (January 1, 2011): 78–88. http://dx.doi.org/10.2174/187152011794941262.

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48

Feldman, Heather, Sonali Arora, Pia Hoellerbauer, Steven Pollard, Anoop Patel, Christopher Plaisier, and Patrick Paddison. "STEM-05. NEURAL G0: A NOVEL QUIESCENT-LIKE STATE IN PROLIFERATING HUMAN NEURAL STEM AND GLIOBLASTOMA TUMOR CELLS." Neuro-Oncology 21, Supplement_6 (November 2019): vi234. http://dx.doi.org/10.1093/neuonc/noz175.979.

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Abstract Single cell (sc) genomic technologies are rapidly transforming our understanding of cellular states in normal and diseased tissues. Here, we applied scRNA-seq to cultures of proliferating human neural stem cells (NSCs) to better understand the relationship between cell cycle dynamics and developmental gene expression. This analysis revealed both conventional cell cycle states (S, G2, M) and novel G1 and G0-like states. Of note, we identified a Neural G0 phase representing a subpopulation enriched for expression of genes associated with adult quiescent NSCs, including CLU, HOPX, ID3, OLIG2, PTN, SYT11, S100B, SOX9, PTPRZ1, and TTYH1. Remarkably, by applying our hNSC cell cycle phase classifier to human glioblastoma (GBM) tumors, we found that Neural G0 subpopulations as a prominent tumor-specific cellular subclass of GBM tumors, which, similar to NSCs, does not overlap with proliferative cell cycle phases. We further identified modulators of Neural G0 via CRISPR-Cas9 screens, revealing highly significant enrichment for tumor suppressor genes associated with brain tumors. In depth analysis of five of these Neural G0 modulatory genes, including CREBBP, NF2, PTPN14, TAOK1, or TP53, revealed that they promote compartmentalization of G0/G1 phase and expression of genes associated with Neural G0. Our results suggest that Neural G0 is a dynamic cell state in mammalian NSCs, that a subset of GBM cells maintain and is modulated by genes commonly found altered in GBM.

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Xia, Tian, Xue-Mei Yi, Xin Wu, Jun Shang, and Hong-Bing Shu. "PTPN1/2-mediated dephosphorylation of MITA/STING promotes its 20S proteasomal degradation and attenuates innate antiviral response." Proceedings of the National Academy of Sciences 116, no. 40 (September 16, 2019): 20063–69. http://dx.doi.org/10.1073/pnas.1906431116.

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Upon cytosolic viral DNA stimulation, cGMP-AMP synthase (cGAS) catalyzes synthesis of 2′3′cGMP-AMP (cGAMP), which binds to the adaptor protein MITA (mediator of IRF3 activation, also called STING, stimulator of IFN genes) and induces innate antiviral response. How the activity of MITA/STING is regulated to avoid excessive innate immune response is not fully understood. Here we identified the tyrosine-protein phosphatase nonreceptor type (PTPN) 1 and 2 as MITA/STING-associated proteins. PTPN1 and PTPN2 are associated with MITA/STING following viral infection and dephosphorylate MITA/STING at Y245. Dephosphorylation of MITA/STING leads to its degradation via the ubiquitin-independent 20S proteasomal pathway, which is dependent on the intrinsically disordered region (IDR) of MITA/STING. Deficiencies of PTPN1 and PTPN2 enhance viral DNA-induced transcription of downstream antiviral genes and innate antiviral response. Our findings reveal that PTPN1/2-mediated dephosphorylation of MITA/STING and its degradation by the 20S proteasomal pathway is an important regulatory mechanism of innate immune response to DNA virus.

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Wingbermühle, Ellen, Renée L. Roelofs, Wouter Oomens, Jennifer Kramer, Jos M. T. Draaisma, Erika Leenders, Tjitske Kleefstra, Roy P. C. Kessels, and Jos I. M. Egger. "Cognitive Phenotype and Psychopathology in Noonan Syndrome Spectrum Disorders through Various Ras/MAPK Pathway Associated Gene Variants." Journal of Clinical Medicine 11, no. 16 (August 13, 2022): 4735. http://dx.doi.org/10.3390/jcm11164735.

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Cognitive difficulties are argued to be common in patients with Noonan syndrome spectrum disorders (NSSDs), but findings are based on studies in which patients with variants in PTPN11 (prevalence ~50%) were overrepresented. The current study, using a structured clinical approach, describes the cognitive phenotype and psychopathology of 100 patients (aged 6 to 61 years) with nine different gene variants in the Ras/MAPK pathway underlying NSSDs (PTPN11n = 61, PTPN11 Noonan syndrome with multiple lentigines n = 3, SOS1n = 14, KRASn = 7, LZTR1n = 5, RAF1n = 4, SHOC2n = 2, CBLn = 2, SOS2n = 2). After weighted assessment and bootstrapping of the results of individual neuropsychological assessments and measures of psychopathology, cognitive performances in most variant groups were within the ranges of expectation. IQs were significantly lower in patients with variants in PTPN11, KRAS, RAF1, and SHOC2, but no specific cognitive impairments were found. The performances of younger participants (<16 years of age) did not differ from those of adults. Alexithymia and internalizing problems were more frequent in patients with variants in PTPN11 and SOS1, while PTPN11 patients also showed higher levels of externalizing problems. These results stress the need to take intelligence into account when interpreting lower cognitive performances in individual neuropsychological assessments, which is crucial for an adequate understanding and guidance of patients with NSSDs.

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