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Contribution of phosphoproteomics in understanding SRC signaling in normal and tumor cells
Author(s) -
Sirvent Audrey,
Urbach Serge,
Roche Serge
Publication year - 2015
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201400162
Subject(s) - proto oncogene tyrosine protein kinase src , signal transduction , microbiology and biotechnology , receptor tyrosine kinase , biology , carcinogenesis , phosphoproteomics , tyrosine kinase , regulator , cell signaling , cancer research , phosphorylation , cancer , biochemistry , protein kinase a , protein phosphorylation , genetics , gene
The membrane‐anchored, non‐receptor tyrosine kinase (non‐RTK) SRC is a critical regulator of signal transduction induced by a large variety of cell‐surface receptors, including RTKs that bind to growth factors to control cell growth and migration. When deregulated, SRC shows strong oncogenic activity, probably because of its capacity to promote RTK‐mediated downstream signaling even in the absence of extracellular stimuli. Accordingly, SRC is frequently deregulated in human cancer and is thought to play important roles during tumorigenesis. However, our knowledge on the molecular mechanism by which SRC controls signaling is incomplete due to the limited number of key substrates identified so far. Here, we review how phosphoproteomic methods have changed our understanding of the mechanisms underlying SRC signaling in normal and tumor cells and discuss how these novel findings can be used to improve therapeutic strategies aimed at targeting SRC signaling in human cancer.