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Article: Receptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp

TitleReceptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp
Authors
Issue Date1994
PublisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/onc
Citation
Oncogene, 1994, v. 9 n. 6, p. 1545-1550 How to Cite?
AbstractThe murine phosphotyrosine phosphatase, Syp, is a widely-expressed cytoplasmic enzyme that contains two SH2 domains. Syp is physically associated with activated receptors for epidermal growth factor (EGF) and platelet-derived growth factor (PDGF), apparently through its SH2 domains. This phosphatase is rapidly phosphorylated in cells treated with PDGF or EGF, and is constitutively phosphorylated in v-src transformed cells. Here we report that either the N-terminal or C-terminal Syp SH2 domain alone bound to the activated βPDGF receptor or EGF-receptor in vitro, and that the two SH2 domains linked together exhibited synergistic binding. Substitution of the Tyr1009 autophosphorylation site in the C-terminal tail of activated βPDGFR with Phe abolished the in vitro binding of either SH2 domain to the activated receptor. A 9 amino acid phosphopeptide corresponding to the Tyr1009 autophosphorylation site of the βPDGFR inhibited association of the Syp SH2 domains with the receptor. These results indicate that the Syp SH2 domains have an intrinsic specificity for the Tyr1009 autophosphorylation site of the βPDGFR that dictates binding of the intact Syp phosphatase, and suggest that both SH2 domains have a related binding specificity. Phosphoamino acid analysis of Syp from PDGF-stimulated cells indicated that PDGF primarily induces Syp phosphorylation on tyrosine residues. The mouse Syp gene has been mapped to chromosome 5F region by the fluorescence in situ hybridization. These findings suggest specific functions for Syp in signal transduction downstream of receptor tyrosine kinases.
Persistent Identifierhttp://hdl.handle.net/10722/44275
ISSN
2015 Impact Factor: 7.932
2015 SCImago Journal Rankings: 4.047
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorFeng, GSen_HK
dc.contributor.authorShen, Ren_HK
dc.contributor.authorHeng, HHQen_HK
dc.contributor.authorTsui, LCen_HK
dc.contributor.authorKazlauskas, Aen_HK
dc.contributor.authorPawson, Ten_HK
dc.date.accessioned2007-09-12T03:50:26Z-
dc.date.available2007-09-12T03:50:26Z-
dc.date.issued1994en_HK
dc.identifier.citationOncogene, 1994, v. 9 n. 6, p. 1545-1550en_HK
dc.identifier.issn0950-9232en_HK
dc.identifier.urihttp://hdl.handle.net/10722/44275-
dc.description.abstractThe murine phosphotyrosine phosphatase, Syp, is a widely-expressed cytoplasmic enzyme that contains two SH2 domains. Syp is physically associated with activated receptors for epidermal growth factor (EGF) and platelet-derived growth factor (PDGF), apparently through its SH2 domains. This phosphatase is rapidly phosphorylated in cells treated with PDGF or EGF, and is constitutively phosphorylated in v-src transformed cells. Here we report that either the N-terminal or C-terminal Syp SH2 domain alone bound to the activated βPDGF receptor or EGF-receptor in vitro, and that the two SH2 domains linked together exhibited synergistic binding. Substitution of the Tyr1009 autophosphorylation site in the C-terminal tail of activated βPDGFR with Phe abolished the in vitro binding of either SH2 domain to the activated receptor. A 9 amino acid phosphopeptide corresponding to the Tyr1009 autophosphorylation site of the βPDGFR inhibited association of the Syp SH2 domains with the receptor. These results indicate that the Syp SH2 domains have an intrinsic specificity for the Tyr1009 autophosphorylation site of the βPDGFR that dictates binding of the intact Syp phosphatase, and suggest that both SH2 domains have a related binding specificity. Phosphoamino acid analysis of Syp from PDGF-stimulated cells indicated that PDGF primarily induces Syp phosphorylation on tyrosine residues. The mouse Syp gene has been mapped to chromosome 5F region by the fluorescence in situ hybridization. These findings suggest specific functions for Syp in signal transduction downstream of receptor tyrosine kinases.en_HK
dc.languageengen_HK
dc.publisherNature Publishing Group. The Journal's web site is located at http://www.nature.com/oncen_HK
dc.relation.ispartofOncogeneen_HK
dc.subject.meshChromosome mappingen_HK
dc.subject.meshIntracellular signaling peptides and proteinsen_HK
dc.subject.meshProtein-tyrosine-phosphatase - genetics - metabolismen_HK
dc.subject.meshReceptor, epidermal growth factor - metabolismen_HK
dc.subject.meshReceptors, platelet-derived growth factor - metabolismen_HK
dc.titleReceptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Sypen_HK
dc.typeArticleen_HK
dc.identifier.emailTsui, LC: tsuilc@hkucc.hku.hken_HK
dc.identifier.authorityTsui, LC=rp00058en_HK
dc.description.naturelink_to_subscribed_fulltexten_HK
dc.identifier.pmid8183548-
dc.identifier.scopuseid_2-s2.0-0028302603en_HK
dc.identifier.volume9en_HK
dc.identifier.issue6en_HK
dc.identifier.spage1545en_HK
dc.identifier.epage1550en_HK
dc.identifier.isiWOS:A1994NL81500004-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridFeng, GS=7401641961en_HK
dc.identifier.scopusauthoridShen, R=7202935786en_HK
dc.identifier.scopusauthoridHeng, HHQ=7005338076en_HK
dc.identifier.scopusauthoridTsui, LC=7102754167en_HK
dc.identifier.scopusauthoridKazlauskas, A=7006235602en_HK
dc.identifier.scopusauthoridPawson, T=35378370700en_HK

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