R3 receptor tyrosine phosphatases: Conserved regulators of receptor tyrosine kinase signaling and tubular organ development

Jeon, Mili; Zinn, Kai

doi:10.1016/j.semcdb.2014.09.005

Cited by 10 publications

(16 citation statements)

References 63 publications

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“…Earlier studies in Drosophila epithelial tissues and mammalian cells showed that Ptp4E and Ptp10D dampen RTK signalling 5,9,49 . Btk29A, on the other hand, is a positive RTK effector 13,15 .…”

Section: Discussionmentioning

confidence: 99%

“…It involves two type III receptor protein tyrosine phosphatases (PTPs), Ptp10D and Ptp4E, the non-receptor tyrosine kinase (non-RTK) Btk29A, and the actin nucleation-promoting factor WASH (Wiskott–Aldrich syndrome protein and SCAR homologue). Type III PTPs contain a single catalytic phosphatase domain in the cytoplasmic region and fibronectin type III-like domains in their extracellular region 5,6 . In Drosophila , Ptp10D and Ptp4E 7 control airway tube shapes through negative regulation of epidermal growth factor receptor (EGFR) signalling 8 .…”

Section: Introductionmentioning

confidence: 99%

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WASH phosphorylation balances endosomal versus cortical actin network integrities during epithelial morphogenesis

et al. 2019

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Filamentous actin (F-actin) networks facilitate key processes like cell shape control, division, polarization and motility. The dynamic coordination of F-actin networks and its impact on cellular activities are poorly understood. We report an antagonistic relationship between endosomal F-actin assembly and cortical actin bundle integrity during Drosophila airway maturation. Double mutants lacking receptor tyrosine phosphatases (PTP) Ptp10D and Ptp4E, clear luminal proteins and disassemble apical actin bundles prematurely. These defects are counterbalanced by reduction of endosomal trafficking and by mutations affecting the tyrosine kinase Btk29A, and the actin nucleation factor WASH. Btk29A forms protein complexes with Ptp10D and WASH, and Btk29A phosphorylates WASH. This phosphorylation activates endosomal WASH function in flies and mice. In contrast, a phospho-mimetic WASH variant induces endosomal actin accumulation, premature luminal endocytosis and cortical F-actin disassembly. We conclude that PTPs and Btk29A regulate WASH activity to balance the endosomal and cortical F-actin networks during epithelial tube maturation.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

WASH phosphorylation balances endosomal versus cortical actin network integrities during epithelial morphogenesis

et al. 2019

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“…It has been proposed that they dephosphorylate tyrosine kinases (RTK) to regulate RTK signaling since most of the known substrates of R3 RPTPs are RTKs [14, 16]. An involvement of these proteins and R3 RPTPs from invertebrate model animals, except PTP52F, in tubular organ development, has been suggested by Jeon and Zinn, 2015 [14].…”

Section: Discussionmentioning

confidence: 99%

“…The specific involvement of vertebrate R3 RPTPs in cancer and other pathologies has been the subject of several recent reports and reviews [ 1 , 4 , 12 , 13 ]. In invertebrates, R3 RPTPs have been functionally characterized in protostome animal models: PTP52F, PTP10D and PTP4e in the fruitfly Drosophila melanogaster and F44G4.8/DEP-1 (nematode.2 sequence in this study) in the nematode Caenorhabditis elegans (reviewed by Jeon and Zinn, 2015) [ 14 ].…”

Section: Introductionmentioning

confidence: 99%

Phosphotyrosine phosphatase R3 receptors: Origin, evolution and structural diversification

2017

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Subtype R3 phosphotyrosine phosphatase receptors (R3 RPTPs) are single-spanning membrane proteins characterized by a unique modular composition of extracellular fibronectin repeats and a single cytoplasmatic protein tyrosine phosphatase (PTP) domain. Vertebrate R3 RPTPs consist of five members: PTPRB, PTPRJ, PTPRH and PTPRO, which dephosphorylate tyrosine residues, and PTPRQ, which dephosphorylates phophoinositides. R3 RPTPs are considered novel therapeutic targets in several pathologies such as ear diseases, nephrotic syndromes and cancer. R3 RPTP vertebrate receptors, as well as their known invertebrate counterparts from animal models: PTP52F, PTP10D and PTP4e from the fruitfly Drosophila melanogaster and F44G4.8/DEP-1 from the nematode Caenorhabditis elegans, participate in the regulation of cellular activities including cell growth and differentiation. Despite sharing structural and functional properties, the evolutionary relationships between vertebrate and invertebrate R3 RPTPs are not fully understood. Here we gathered R3 RPTPs from organisms covering a broad evolutionary distance, annotated their structure and analyzed their phylogenetic relationships. We show that R3 RPTPs (i) have probably originated in the common ancestor of animals (metazoans), (ii) are variants of a single ancestral gene in protostomes (arthropods, annelids and nematodes); (iii) a likely duplication of this ancestral gene in invertebrate deuterostomes (echinodermes, hemichordates and tunicates) generated the precursors of PTPRQ and PTPRB genes, and (iv) R3 RPTP groups are monophyletic in vertebrates and have specific conserved structural characteristics. These findings could have implications for the interpretation of past studies and provide a framework for future studies and functional analysis of this important family of proteins.

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“…Soady et al showed that PTPRB negatively regulates branching morphogenesis in the mammary epithelium, dependent on inhibition of FGFR activation and ERK1/2 phosphorylation 9 . Genetic studies in both mammals and invertebrate model systems have shown that the RPTP family is essential for tubular organ development 10 .…”

Section: Introductionmentioning

confidence: 99%

PTPRB promotes metastasis of colorectal carcinoma via inducing epithelial-mesenchymal transition

Weng

Chen

et al. 2019

Cell Death Dis

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Dysregulation of protein tyrosine phosphatase, receptor type B (PTPRB) correlates with the development of a variety of tumors. Here we show that PTPRB promotes metastasis of colorectal cancer (CRC) cells via inducing epithelial-mesenchymal transition (EMT). We find that PTPRB is expressed at significantly higher levels in CRC tissues compared to adjacent nontumor tissues and in CRC cell lines with high invasion. PTPRB knockdown decreased the number of invasive CRC cells in an in vitro wound healing model, and also reduced tumor metastasis in vivo. Conversely, PTPRB overexpression promoted CRC cell invasion in vitro and metastasis in vivo. PTPRB overexpression decreased vimentin expression and promoted E-cadherin expression, consistent with promotion of EMT, while PTPRB knockdown had the opposite effect. Hypoxic conditions induced EMT and promoted invasion in CRC cells, but these effects were eliminated by PTPRB knockdown. EMT blockade via TWIST1 knockdown inhibited the migration and invasiveness of CRC cells, and even increased PTPRB expression could not reverse this effect. Altogether, these data support the conclusion that PTPRB promotes invasion and metastasis of CRC cells via inducing EMT, and that PTPRB would be a novel therapeutic target for the treatment of CRC.

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R3 receptor tyrosine phosphatases: Conserved regulators of receptor tyrosine kinase signaling and tubular organ development

Cited by 10 publications

References 63 publications

WASH phosphorylation balances endosomal versus cortical actin network integrities during epithelial morphogenesis

WASH phosphorylation balances endosomal versus cortical actin network integrities during epithelial morphogenesis

Phosphotyrosine phosphatase R3 receptors: Origin, evolution and structural diversification

PTPRB promotes metastasis of colorectal carcinoma via inducing epithelial-mesenchymal transition

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