Exploring monomerization of ErbB receptor dimers as a mechanism offeedback regulation employing correlation spectroscopy

The cells in the body frequently interact with each other deciding the share of resources, growth and death. Often these communications are conveyed through small proteins like epidermal growth factor (EGF). The signal from EGF is received by a receptor that binds to EGF on the cell surface, and ultimately activates the processes needed for growth. EGF and the EGF receptor are part of a family of proteins that include four receptors, collectively termed ErbB/HER receptors, and protein signals such as amphiregulin. These signals and receptors can mix and match, with different messages bringing together two identical or two different receptors yielding a dimeric complex. In this way, a wide variety of messages may be carried by the system, tailored for the needs of each type of cell. The way the receptors interact can be dynamic and are responsible for regulation of the cell signaling, but the dynamics of the interaction (especially the dimer formation) remains to be explored. This project aims to investigate the dynamics of different ErbB receptor dimeric complexes in live cells by employing advanced microscopic techniques and to study how they relay the message to signaling proteins. The defective ErbB receptors have been found in diseases like breast cancer. Thus, the outcome of this research will help to understand better the activation of these receptors and will serve as a foundation for medical applications, especially for developing new mode of anti-cancer drugs.