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PTPRE — SRC
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Gil-Henn et al., J Biol Chem 2003
(Mammary Neoplasms, Experimental) :
We show that at the molecular level,
RPTPepsilon activates
Src , a known collaborator of Neu in mammary tumorigenesis ... Lack of
RPTPepsilon reduced
Src activity and altered Src phosphorylation in tumor cells ; RPTPepsilon dephosphorylated and activated Src ; and Src bound a substrate trapping mutant of RPTPepsilon ... We conclude that
RPTPepsilon is a physiological
activator of
Src in Neu induced mammary tumors and suggest that pharmacological inhibition of phosphatases that activate Src may be useful to augment direct pharmacological inhibition of Src
Berman-Golan et al., Oncogene 2007
(Mammary Neoplasms, Experimental) :
Neu mediated phosphorylation of
protein tyrosine phosphatase epsilon is
critical for activation of
Src in mammary tumor cells ... The receptor-type
protein tyrosine phosphatase epsilon ( RPTPepsilon )
activates c-Src in mammary tumor cells induced in vivo by Neu ... However, the molecular mechanisms that control
activation of
c-Src by
RPTPepsilon are unknown ... We show that Neu induces phosphorylation of RPTPepsilon exclusively at its C-terminal Y695, and that this phosphorylation is required for
activation of
c-Src by
RPTPepsilon
Berman-Golan et al., Cancer Metastasis Rev 2008
(Cell Transformation, Neoplastic...) :
At the molecular level,
RPTPepsilon dephosphorylates and
activates Src and the related kinases Yes and Fyn, and the activities of these kinases are significantly reduced in tumor cells lacking RPTPepsilon ... This event is crucial in enabling
RPTPepsilon to
activate Src , but appears not to affect the activity of RPTPepsilon towards unrelated substrates
Granot-Attas et al., Mol Biol Cell 2009
:
Protein tyrosine phosphatase epsilon regulates integrin mediated podosome stability in osteoclasts by activating
Src