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TitleCryo-EM structure of the activated RET signaling complex reveals the importance of its cysteine-rich domain.
Journal, issue, pagesSci Adv, Vol. 5, Issue 7, Page eaau4202, Year 2019
Publish dateJul 31, 2019
AuthorsJanna M Bigalke / Shintaro Aibara / Robert Roth / Göran Dahl / Euan Gordon / Sarah Dorbéus / A Amunts / Jenny Sandmark /
PubMed AbstractSignaling through the receptor tyrosine kinase RET is essential during normal development. Both gain- and loss-of-function mutations are involved in a variety of diseases, yet the molecular details ...Signaling through the receptor tyrosine kinase RET is essential during normal development. Both gain- and loss-of-function mutations are involved in a variety of diseases, yet the molecular details of receptor activation have remained elusive. We have reconstituted the complete extracellular region of the RET signaling complex together with Neurturin (NRTN) and GFRα2 and determined its structure at 5.7-Å resolution by cryo-EM. The proteins form an assembly through RET-GFRα2 and RET-NRTN interfaces. Two key interaction points required for RET extracellular domain binding were observed: (i) the calcium-binding site in RET that contacts GFRα2 domain 3 and (ii) the RET cysteine-rich domain interaction with NRTN. The structure highlights the importance of the RET cysteine-rich domain and allows proposition of a model to explain how complex formation leads to RET receptor dimerization and its activation. This provides a framework for targeting RET activity and for further exploration of mechanisms underlying neurological diseases.
External linksSci Adv / PubMed:31392261 / PubMed Central
MethodsEM (single particle)
Resolution6.3 Å
Structure data

EMDB-0026, PDB-6gl7:
Neurturin-GFRa2-RET extracellular complex
Method: EM (single particle) / Resolution: 6.3 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / Neurotrophic signalling / Receptor tyrosine kinase / GDNF family of ligands

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