The Proteomics of Posttranslational Modifications: Unraveling Cellular Signaling Through Mass Spectrometry
Event Date: June 8, 2011 12 noon Eastern, 9 a.m. Pacific, 5 p.m. UK, 6 p.m. CEST
Sponsored by Cell Signaling Technology
Posttranslational modifications—including phosphorylation, acetylation, and ubiquitination—allow for the fine-tuning of signaling pathways and networks within cells. Mass spectrometry-based proteomics techniques are powerful tools for the investigation of these networks. Dynamic protein phosphorylation is a key cellular regulatory mechanism, and the characterization of global phosphorylation profiles using large-scale proteomic approaches, including antibody-based phosphopeptide enrichment, has proven informative. Acetylation has also been studied using these approaches—as histone deacetylase inhibitors gain clinical importance, the need to better characterize their mechanism of action has accelerated lysine acetylation proteomics research. Further, ubiquitination is gaining growing attention as an important mechanism for both signal transduction and proteolytic degradation. Most recently, new ubiquitin affinity reagents, such as the ubiquitin remnant antibody, have become available, allowing for the identification of hundreds of ubiquitinylated lysine residues in human cells.
During this webinar, viewers will:
- Obtain an overview of posttranslational mechanisms and their role in cellular signaling
- Learn about technologies for studying and characterizing these modifications
- See how the latest technologies are being applied by experts in the field to cellular signaling research
- Have the opportunity to put their question to the expert panel live and in real time.
Register HERE for the webinar!
Follow
If you enjoyed this article, please consider sharing it!
