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RET receptor tyrosine kinase architecture, assemblies, and activation
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DOI：10.1530/ERC-25-0322.png)
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Abstract
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Among the 58 human receptor tyrosine kinases that are known, only the RET (REarrangement during Transfection) receptor contains cadherin-like domains in its extracellular portion. This multidomain extracellular module contains a binding site for a family of five related heterodimeric ligands. Each heterodimer comprises a secreted glial cell line-derived neurotrophic factor (GDNF) family ligand (GFL) and a membrane-anchored co-receptor GFR alpha (GDNF family receptor alpha). Once a GFL-GFR alpha ligand is bound to RET, this stimulates the activation of the receptor through tyrosine-based autophosphorylation. This mini review explores how the shape and architecture of RET encode a flexible GFL-GFR alpha-binding site, summarising recent progress in understanding RET structure. It then discusses current views on how distinct assemblies of GFL-GFR alpha-RET receptor complexes are able to activate the intrinsic RET tyrosine kinase function to relay intracellular signals.
Keywords:
growth factor receptor
cell signalling
neurotrophic factor
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