Receptor‐type tyrosine phosphatase ligands: looking for the needle in the haystack

Mohebiany, Alma N.; Nikolaienko, Roman; Bouyain, Samuel; Harroch, Sheila

doi:10.1111/j.1742-4658.2012.08653.x

Cited by 44 publications

(34 citation statements)

References 114 publications

(169 reference statements)

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“…Three fusion transcripts contained sequences encoding the carbonic anhydrase (CA) domain and fibronectin type III (Fib III) domain of PTPRZ1 (Mohebiany et al 2013) fused to the dimerization domain, immunoglobulin-like domains, transmembrane domain, and the tyrosine kinase domain of MET ( Fig. 2A; Organ and Tsao 2011).…”

Section: Validation Of the Ptprz1-met As A Recurrent Fusion Transcriptmentioning

confidence: 99%

RNA-seq of 272 gliomas revealed a novel, recurrent PTPRZ1-MET fusion transcript in secondary glioblastomas

et al. 2014

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Studies of gene rearrangements and the consequent oncogenic fusion proteins have laid the foundation for targeted cancer therapy. To identify oncogenic fusions associated with glioma progression, we catalogued fusion transcripts by RNA-seq of 272 gliomas. Fusion transcripts were more frequently found in high-grade gliomas, in the classical subtype of gliomas, and in gliomas treated with radiation/temozolomide. Sixty-seven in-frame fusion transcripts were identified, including three recurrent fusion transcripts: FGFR3-TACC3, RNF213-SLC26A11, and PTPRZ1-MET (ZM). Interestingly, the ZM fusion was found only in grade III astrocytomas (1/13; 7.7%) or secondary GBMs (sGBMs, 3/20; 15.0%). In an independent cohort of sGBMs, the ZM fusion was found in three of 20 (15%) specimens. Genomic analysis revealed that the fusion arose from translocation events involving introns 3 or 8 of PTPRZ and intron 1 of MET. ZM fusion transcripts were found in GBMs irrespective of isocitrate dehydrogenase 1 (IDH1) mutation status. sGBMs harboring ZM fusion showed higher expression of genes required for PIK3CA signaling and lowered expression of genes that suppressed RB1 or TP53 function. Expression of the ZM fusion was mutually exclusive with EGFR overexpression in sGBMs. Exogenous expression of the ZM fusion in the U87MG glioblastoma line enhanced cell migration and invasion. Clinically, patients afflicted with ZM fusion harboring glioblastomas survived poorly relative to those afflicted with non-ZM-harboring sGBMs (P < 0.001). Our study profiles the shifting RNA landscape of gliomas during progression and reveled ZM as a novel, recurrent fusion transcript in sGBMs.

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Section: Validation Of the Ptprz1-met As A Recurrent Fusion Transcriptmentioning

confidence: 99%

RNA-seq of 272 gliomas revealed a novel, recurrent PTPRZ1-MET fusion transcript in secondary glioblastomas

et al. 2014

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“…Since their extracellular domains are similar in structure to the extracellular domains found in cell adhesion molecules RPTPs appear to be involved in cell-cell and cell-matrix communications [7]. Typically, ligand binding to the extracellular domain of an RPTP induces dimerization that leads to the inhibition of its catalytic activity [16-19].…”

Section: The Ptp Superfamilymentioning

confidence: 99%

“…Comprehensive reviews also exist on PTPs in human cancer [5] and the involvement of lipid-phosphatases in human disease [6]. RPTPs and the biological insight uncovered by the solution of several RPTP crystal structures have also been topics of discussion [7, 8]. We direct the reader to these sources for more comprehensive discussions since this review will focus largely on the application of non-biased screens as a discovery tool for PTP function.…”

Section: Introductionmentioning

confidence: 99%

Mining the function of protein tyrosine phosphatases in health and disease

Lee

Lawan

et al. 2015

Seminars in Cell & Developmental Biology

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Protein tyrosine phosphatases (PTPs) play a crucial role in the regulation of human health and it is now clear that PTP dysfunction is causal to a variety of human diseases. Research in the PTP field has accelerated dramatically over the last decade fueled by cutting-edge technologies in genomic and proteomic techniques. This system-wide non-biased approach when applied to the discovery of PTP function has led to the elucidation of new and unanticipated roles for the PTPs. These discoveries, driven by genomic and proteomic approaches, have uncovered novel PTP findings that range from those that describe fundamental cell signaling mechanisms to implications for PTPs as novel therapeutic targets for the treatment of human disease. This review will discuss how new PTP functions have been uncovered through studies that have utilized genomic and proteomic technologies and strategies.

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“…This predicts regulatory potential for any biomolecule that would bind to the PTPBR7 and/or PTP-SL parts that are N-terminal of the transmembrane segment. Identification of receptortype PTP ligands is a cumbersome process (Stoker, 2005;Mohebiany et al, 2013) and although mouse PTPBR7 extracellular domain displayed a clear affinity for highly myelinated brain regions (Chesini et al, 2011) the corresponding PTPRR ligands still await proper identification.…”

Section: Localisationmentioning

confidence: 99%