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SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
1Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.
Abstract:
A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. Furthermore, Syp was constitutively phosphorylated on tyrosine in cells transformed by v-src. This mammalian phosphatase is most closely related, especially in its SH2 domains, to the corkscrew (csw) gene product of Drosophila, which is required for signal transduction downstream of the Torso receptor tyrosine kinase. The Syp gene is widely expressed throughout embryonic mouse development and in adult tissues. Thus, Syp may function in mammalian embryonic development and as a common target of both receptor and nonreceptor tyrosine kinases.
Insights
Scientists discovered Syp, a mouse phosphotyrosine phosphatase with two Src homology 2 domains. Syp interacts with growth factor receptors and may play a role in embryonic development and signal transduction.
Area of Science:
- Molecular Biology
- Biochemistry
- Developmental Biology
Background:
- Tyrosine kinases are crucial in cell signaling pathways.
- Phosphatases play a key role in regulating tyrosine kinase activity.
- Understanding novel phosphatases is essential for deciphering complex cellular processes.
Purpose of the Study:
- To identify and characterize a novel mouse phosphotyrosine phosphatase.
- To investigate the interaction of this phosphatase with receptor tyrosine kinases.
- To explore its potential role in mammalian development and signal transduction.
Main Methods:
- Identification of the Syp phosphatase.
- Analysis of Syp's interaction with epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors using its Src homology 2 (SH2) domains.
- Assessment of Syp phosphorylation in stimulated and transformed cells.
Main Results:
- A novel mouse phosphotyrosine phosphatase, Syp, containing two SH2 domains was identified.
- Syp binds to autophosphorylated EGF and PDGF receptors.
- Syp is rapidly phosphorylated on tyrosine in EGF- and PDGF-stimulated cells and constitutively phosphorylated in v-src-transformed cells.
- Syp shows homology to Drosophila corkscrew (csw), a regulator of Torso receptor tyrosine kinase signaling.
- The Syp gene is widely expressed in embryonic and adult mouse tissues.
Conclusions:
- Syp functions as a key regulator in mammalian signal transduction pathways.
- Syp acts as a common target for both receptor and nonreceptor tyrosine kinases.
- Syp is likely involved in mammalian embryonic development.