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Literate Review: A survey of protein kinases and phosphatases in lung cancer
Summary/scope (100 words)
The molecular defects that cause the development of cancer remain unknown. Cells respond to changes in their extracellular surroundings and maintain cellular homeostasis largely through signalling mechanisms or networks involving posttranslational protein modifications. This well-coordinated and subtly balanced signalling network is distorted in tumours, where cell proliferation and survival are strengthened and apoptosis is impaired. The study of complex signalling networks to identify alterations in cells that lead to disease has been aided greatly aided by the availability of chemical and biochemical tools (inhibitors, antibodies etc.) in recent years.
Justification/unmet need (100 words)
A key posttranslational protein modification that regulates many cellular signalling pathways and functions is reversible protein phosphorylation. Despite the success of tyrosine kinase-based cancer therapeutics, for most tumours the kinases and phosphatases that drive disease remain unknown, limiting our ability to identify drug targets and predict response. This review will survey the role of protein phosphorylation across breast or lung cancer cell lines and solid tumours in order to classify them based upon aberrant kinases and phosphatases.
Three recent (<5 years old) references 1) Beltran L, Casado P, Rodríguez-Prados J, Cutillas P R. (2012), Global profiling of protein kinase activities in cancer cells by mass spectrometry, Journal of Proteomics Vol 77, Pages 492–503. 2) Sun T, Aceto N, Meerbrey K L. et al. (2011) Activation of Multiple Proto-oncogenic Tyrosine Kinases in Breast Cancer via Loss of the PTPN12 Phosphatase Cell, Vol 144(5), Pages 703-718. 3) H.C. Harsha, Pandey A (2010) Phosphoproteomics in cancer Molecular Oncology, Vol 4(6), Pages 482-495. [meteor_slideshow slideshow="best" metadata="height: 126, width: 630"]