Growth Factors and Receptor Tyrosine Kinases in Development, Regeneration, and Tumorigenesis

Dear Colleagues,

Members of the family of receptor tyrosine kinases (RTKs) have been shown to have important functions in embryonal development, wound healing, and tissue homeostasis. Based on their structural properties, the 58 members of the family can be divided in 20 subfamilies; their extracellular ligand-binding parts are composed of different combinations of domains, including immunoglobulin-like, epidermal growth factor-like, fibronectin-like, cysteine-rich, cadherin-like, and discoidin-like domains, and their intracellular parts contain intrinsic tyrosine-kinase domains.

Many, maybe all, RTKs are activated by dimerization or oligomerization, induced by ligand binding. This results in the auto-phosphorylation of certain tyrosine residues in the intracellular parts of the receptors, creating docking sites for SH2-domain-containing molecules, as well as in the tyrosine phosphorylation of specific downstream signaling molecules. The activated signaling pathways leads to the stimulation of cell growth, survival, and migration. Over-activity, by mutation, amplification, or overexpression, of RTKs are common in tumorigenesis, and more than half of the known RTKs have been implicated as drivers of various types of tumors. Tyrosine kinase inhibitors have therefore been developed and are used clinically, with beneficial effects in the treatment of certain tumors.

This Special Issue will highlight recent developments in our understanding about the normal function of RTKs and their role in disease, as well as their structural properties.

Prof. Dr. Carl-Henrik Heldin
Guest Editor

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