Mechanisms of Signal Transduction
Mechanisms of Cell Growth and Autophagy Regulation
Protein Phosphorylation Networks
G-proteins in Cellular Regulation
Mechanisms of Signaling Specificity in Cell Fate: Growth, Proliferation or Death?
For more details, go to the ASBMB Meeting 2013 program page
and click to expland “Mechanisms of Signal Transduction.”
How do cells select and translate myriad signals into specific biological responses?
Understanding the full complexity of signal transduction is essential to understanding the many contexts for altered signaling, such as pathophysiological conditions related to stress or the development of cancer. Sessions within this broad theme will cover new findings in autophagy signaling, protein kinases and phosphatases, G-protein–coupled receptor signaling and mechanisms of cell-signaling specificity in cell fate.
Highlights of the session on autophagy include details of the biochemical mechanisms and cell biology of autophagy machinery regulation, including novel aspects of the VPS34 lipid kinase complex function and regulation in response to nutrient signals.
Protein phosphorylation is a fundamental regulatory mechanism that affects nearly every aspect of cellular behavior. Recent findings from the Dixon lab (Tagliabracci et al., Science 2012) reveal that protein kinases are not confined to the cell interior: A family of Golgi-localized protein kinases are secreted and phosphorylate extracellular proteins implicated in bone biomineralization. The G-protein–coupled-receptor session will highlight not only the recent progress in the mechanistic understanding of GPCR signaling but also will cover the relevance of GPCR dysregulation to the development of human diseases.
A final session will deal with mechanisms of signaling specificity and cell fate. The strength and duration of signaling can have profound effects on signaling output; cells reuse the same pathways in subtly different ways to regulate disparate biologies.
Related to this theme, the ser/thr protein kinase mTOR, the mammalian target of rapamycin, plays a critical role in many pathophysiological processes. The Blenis lab (Yu et al., Science 2011) has discovered a tumor-suppressive role for Grb10, a novel mTOR substrate that, when phosphorylated, inhibits both PI3K and ERK-MAPK signaling. Loss of Grb10 may contribute to the elevated signaling and altered cell fate that typify cancer.
Kun-Liang Guan (firstname.lastname@example.org) is a professor of pharmacology at the University of California, San Diego. Carol Lange (email@example.com) is a professor in the departments of medicine and pharmacology at the Masonic Cancer Center at the University of Minnesota.