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A Global Analysis of the Receptor Tyrosine Kinase-Protein Phosphatase Interactome
- Source :
- Molecular Cell. 65:347-360
- Publication Year :
- 2017
- Publisher :
- Elsevier BV, 2017.
-
Abstract
- Receptor tyrosine kinases (RTKs) and protein phosphatases comprise protein families that play crucial roles in cell signaling. We used two protein-protein interaction (PPI) approaches, the Membrane Yeast Two-Hybrid (MYTH) and the Mammalian Membrane Two-Hybrid (MaMTH), to map the PPIs between human RTKs and phosphatases. The resulting RTK-phosphatase interactome reveals a considerable number of previously unidentified interactions and suggests specific roles for different phosphatase families. Additionally, the differential PPIs of some protein tyrosine phosphatases (PTPs) and their mutants suggest diverse mechanisms of these PTPs in the regulation of RTK signaling. We further found that PTPRH and PTPRB directly dephosphorylate EGFR and repress its downstream signaling. By contrast, PTPRA plays a dual role in EGFR signaling: besides facilitating EGFR dephosphorylation, it enhances downstream ERK signaling by activating SRC. This comprehensive RTK-phosphatase interactome study provides a broad and deep view of RTK signaling.
- Subjects :
- 0301 basic medicine
Phosphatase
Protein tyrosine phosphatase
Transfection
Interactome
Article
Receptor tyrosine kinase
PTPRB
Mice
03 medical and health sciences
0302 clinical medicine
Two-Hybrid System Techniques
Protein Interaction Mapping
Animals
Humans
Protein Interaction Maps
Phosphorylation
Molecular Biology
Epidermal Growth Factor
biology
Receptor-Like Protein Tyrosine Phosphatases, Class 4
Receptor-Like Protein Tyrosine Phosphatases, Class 3
Reproducibility of Results
Cell Biology
Enzyme Activation
ErbB Receptors
HEK293 Cells
src-Family Kinases
030104 developmental biology
Biochemistry
030220 oncology & carcinogenesis
Mutation
biology.protein
Signal transduction
Signal Transduction
Proto-oncogene tyrosine-protein kinase Src
Subjects
Details
- ISSN :
- 10972765
- Volume :
- 65
- Database :
- OpenAIRE
- Journal :
- Molecular Cell
- Accession number :
- edsair.doi.dedup.....54b0953e7deea20dd10ca68384733932