期刊
MOLECULAR CELL
卷 65, 期 2, 页码 347-360出版社
CELL PRESS
DOI: 10.1016/j.molcel.2016.12.004
关键词
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资金
- Ontario Research Fund [GL2-01-018, GL2-01-030]
- Canadian Cancer Society Research Institute (CCSRI) [702109, 703889]
- Canadian Cystic Fibrosis Foundation (CFC) [2847]
- Genome Canada/Ontario Genomics [9427, 9428]
- Pancreatic Cancer Canada
- Natural Sciences Research Council (NSERC) [203475]
- Canada Research Chair Program (CRC) [203373, 225404]
- Canada Foundation for Innovation (CFI) [203373, 225404, 12301, 29272, 30865]
- US Army DOD [W81XWH-12-1-0501]
- IBM
- Canadian Institutes of Health Research [FDN 143301, MOP12592, 132191]
- Princess Margaret Cancer Foundation
- [R37 CA49132]
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 RTKphosphatase 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.
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