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http://purl.uniprot.org/citations/17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17130234http://www.w3.org/2000/01/rdf-schema#comment"The protein tyrosine phosphatase PEST (PTP-PEST) is involved in the regulation of the actin cytoskeleton. Despite the emerging functions attributed to both PTPs and the actin cytoskeleton in apoptosis, the involvement of PTP-PEST in apoptotic cell death remains to be established. Using several cell-based assays, we showed that PTP-PEST participates in the regulation of apoptosis. As apoptosis progressed, a pool of PTP-PEST localized to the edge of retracting lamellipodia. Expression of PTP-PEST also sensitized cells to receptor-mediated apoptosis. Concertedly, specific degradation of PTP-PEST was observed during apoptosis. Pharmacological inhibitors, immunodepletion experiments, and in vitro cleavage assays identified caspase-3 as the primary regulator of PTP-PEST processing during apoptosis. Caspase-3 specifically cleaved PTP-PEST at the (549)DSPD motif and generated fragments, some of which displayed increased catalytic activity. Moreover, caspase-3 regulated PTP-PEST interactions with paxillin, leupaxin, Shc, and PSTPIP. PTP-PEST acted as a scaffolding molecule connecting PSTPIP to additional partners: paxillin, Shc, Csk, and activation of caspase-3 correlated with the modulation of the PTP-PEST adaptor function. In addition, cleavage of PTP-PEST facilitated cellular detachment during apoptosis. Together, our data demonstrate that PTP-PEST actively contributes to the cellular apoptotic response and reveal the importance of caspases as regulators of PTPs in apoptosis."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.org/dc/terms/identifier"doi:10.1128/mcb.02462-05"xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Meng T.C."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Tremblay M.L."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Liu Y.C."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Hardy S."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Bourdeau A."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Halle M."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Blanchetot C."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/author"Theberge J.F."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/name"Mol Cell Biol"xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/pages"1172-1190"xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/title"Caspase-3 regulates catalytic activity and scaffolding functions of the protein tyrosine phosphatase PEST, a novel modulator of the apoptotic response."xsd:string
http://purl.uniprot.org/citations/17130234http://purl.uniprot.org/core/volume"27"xsd:string
http://purl.uniprot.org/citations/17130234http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17130234
http://purl.uniprot.org/citations/17130234http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17130234
http://purl.uniprot.org/uniprot/#_D3YWA4-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_F6Z0X5-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_B4E105-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_D6RDQ3-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_D6RGL8-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_D6RGT2-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234
http://purl.uniprot.org/uniprot/#_Q16128-mappedCitation-17130234http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17130234