Help Privacy Policy Disclaimer
  Advanced SearchBrowse




Book Chapter

Phosphoproteomic analysis of signaling pathways in lymphomas.


Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available

Häupl, B., Urlaub, H., & Oellerich, T. (2019). Phosphoproteomic analysis of signaling pathways in lymphomas. In R. Küppers (Ed.), Lymphoma (pp. 371-381).

Cite as: https://hdl.handle.net/21.11116/0000-0003-0A7C-8
Cell fate decisions are controlled by complex signal transduction processes that transmit information via posttranslational protein modifications such as phosphorylation. In lymphoma, as in other cancer types, these signaling networks are often dysregulated and thus contribute to malignant transformation and tumor maintenance. For example, B-cell antigen receptor signals are rewired in certain lymphoma types, such as diffuse large B-cell lymphomas, to promote cell growth and survival of the malignant cell clones. Hence, global elucidation of such intricate signaling networks is important for an improved understanding of the biology of these tumors and the identification of target proteins for therapeutic purposes.We describe here a mass spectrometry-based phosphoproteomic approach for characterization of intracellular signaling events and their dynamics. This integrated phosphoproteomic technology combines phosphopeptide enrichment and fractionation with liquid-chromatography-coupled mass spectrometry for the site-specific mapping and quantification of thousands of phosphorylation events in a given cell type. Such global signaling analyses provide valuable insights into oncogenic signaling networks and can inform drug development efforts.