期刊
EMBO REPORTS
卷 23, 期 6, 页码 -出版社
WILEY
DOI: 10.15252/embr.202154041
关键词
RTK; interaction proteomics; systems biology; receptor tyrosine kinase; phosphoproteomics
资金
- Academy of Finland [288475, 294173]
- Sigrid Juselius Foundation
- Finnish Cancer Foundation
- University of Helsinki Three-year Research Grant
- Biocentrum Helsinki
- Biocentrum Finland
- HiLIFE
- Magnus Ehrnrooth Foundation
- Instrumentarium Research Foundation
- ProjektDEAL
- Academy of Finland (AKA) [294173, 288475, 294173, 288475] Funding Source: Academy of Finland (AKA)
Cell-to-cell communication is facilitated by cell surface receptor tyrosine kinases (RTKs), which phosphorylate downstream substrates in response to stimuli. Through three methods, we have mapped the molecular context and substrate profiles of RTKs, identifying new insights into their functions and interactions.
Much cell-to-cell communication is facilitated by cell surface receptor tyrosine kinases (RTKs). These proteins phosphorylate their downstream cytoplasmic substrates in response to stimuli such as growth factors. Despite their central roles, the functions of many RTKs are still poorly understood. To resolve the lack of systematic knowledge, we apply three complementary methods to map the molecular context and substrate profiles of RTKs. We use affinity purification coupled to mass spectrometry (AP-MS) to characterize stable binding partners and RTK-protein complexes, proximity-dependent biotin identification (BioID) to identify transient and proximal interactions, and an in vitro kinase assay to identify RTK substrates. To identify how kinase interactions depend on kinase activity, we also use kinase-deficient mutants. Our data represent a comprehensive, systemic mapping of RTK interactions and substrates. This resource adds information regarding well-studied RTKs, offers insights into the functions of less well-studied RTKs, and highlights RTK-RTK interactions and shared signaling pathways.
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