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- Scopus: eid_2-s2.0-0028302603
- PMID: 8183548
- WOS: WOS:A1994NL81500004
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Article: Receptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp
Title | Receptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp |
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Authors | |
Issue Date | 1994 |
Publisher | Nature 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? |
Abstract | The 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 Identifier | http://hdl.handle.net/10722/44275 |
ISSN | 2023 Impact Factor: 6.9 2023 SCImago Journal Rankings: 2.334 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Feng, GS | en_HK |
dc.contributor.author | Shen, R | en_HK |
dc.contributor.author | Heng, HHQ | en_HK |
dc.contributor.author | Tsui, LC | en_HK |
dc.contributor.author | Kazlauskas, A | en_HK |
dc.contributor.author | Pawson, T | en_HK |
dc.date.accessioned | 2007-09-12T03:50:26Z | - |
dc.date.available | 2007-09-12T03:50:26Z | - |
dc.date.issued | 1994 | en_HK |
dc.identifier.citation | Oncogene, 1994, v. 9 n. 6, p. 1545-1550 | en_HK |
dc.identifier.issn | 0950-9232 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/44275 | - |
dc.description.abstract | The 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.language | eng | en_HK |
dc.publisher | Nature Publishing Group. The Journal's web site is located at http://www.nature.com/onc | en_HK |
dc.relation.ispartof | Oncogene | en_HK |
dc.subject.mesh | Chromosome mapping | en_HK |
dc.subject.mesh | Intracellular signaling peptides and proteins | en_HK |
dc.subject.mesh | Protein-tyrosine-phosphatase - genetics - metabolism | en_HK |
dc.subject.mesh | Receptor, epidermal growth factor - metabolism | en_HK |
dc.subject.mesh | Receptors, platelet-derived growth factor - metabolism | en_HK |
dc.title | Receptor-binding, tyrosine phosphorylation and chromosome localization of the mouse SH2-containing phosphotyrosine phosphatase Syp | en_HK |
dc.type | Article | en_HK |
dc.identifier.email | Tsui, LC: tsuilc@hkucc.hku.hk | en_HK |
dc.identifier.authority | Tsui, LC=rp00058 | en_HK |
dc.description.nature | link_to_subscribed_fulltext | en_HK |
dc.identifier.pmid | 8183548 | - |
dc.identifier.scopus | eid_2-s2.0-0028302603 | en_HK |
dc.identifier.volume | 9 | en_HK |
dc.identifier.issue | 6 | en_HK |
dc.identifier.spage | 1545 | en_HK |
dc.identifier.epage | 1550 | en_HK |
dc.identifier.isi | WOS:A1994NL81500004 | - |
dc.publisher.place | United Kingdom | en_HK |
dc.identifier.scopusauthorid | Feng, GS=7401641961 | en_HK |
dc.identifier.scopusauthorid | Shen, R=7202935786 | en_HK |
dc.identifier.scopusauthorid | Heng, HHQ=7005338076 | en_HK |
dc.identifier.scopusauthorid | Tsui, LC=7102754167 | en_HK |
dc.identifier.scopusauthorid | Kazlauskas, A=7006235602 | en_HK |
dc.identifier.scopusauthorid | Pawson, T=35378370700 | en_HK |
dc.identifier.issnl | 0950-9232 | - |