SH2 and SH3 Domains: Cellular Signalling and Diseases
A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Signaling".
Deadline for manuscript submissions: closed (28 February 2021) | Viewed by 13129
Special Issue Editor
Special Issue Information
Dear Colleagues,
SH2 and SH3 domains are small noncatalytic protein modules that are conserved among a series of proteins. They couple growth factor receptors to intracellular signal transduction pathways by mediating protein–protein interactions. While SH2 domains bind tyrosine-phosphorylated polypeptides, SH3 domains interact with ligands that possess short proline-rich motifs. It has been well-established how enzymes such as the Src tyrosine kinase family, phospholipase C-gamma, or STAT proteins are regulated by the assistance of SH2 and SH3 domains. These domains are also present in proteins without any catalytic activity, including adaptor, anchor, docking, or scaffold proteins, which serve to link tyrosine kinases to specific target proteins. Although the basal mechanism of action of SH2 and SH3 domains has been well-known for some time, recent findings have suggested a role of both SH2 and SH3 domains in lipid binding. In addition, direct tyrosine phosphorylation of the SH3 domains has emerged as a novel regulatory mechanism.
In this Special Issue, we will provide an open access platform for reviews and original research papers describing all aspects of research on SH2 and SH3 domains.
Prof. Dr. Laszlo BudayGuest Editor
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Keywords
- SH2 and SH3 domains
- Tyrosine kinases
- Phosphorylation
- Protein–protein interactions
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