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TitleA two-site flexible clamp mechanism for RET-GDNF-GFRα1 assembly reveals both conformational adaptation and strict geometric spacing.
Journal, issue, pagesStructure, Vol. 29, Issue 7, Page 694-708.e7, Year 2021
Publish dateJul 1, 2021
AuthorsSarah E Adams / Andrew G Purkiss / Phillip P Knowles / Andrea Nans / David C Briggs / Annabel Borg / Christopher P Earl / Kerry M Goodman / Agata Nawrotek / Aaron J Borg / Pauline B McIntosh / Francesca M Houghton / Svend Kjær / Neil Q McDonald /
PubMed AbstractRET receptor tyrosine kinase plays vital developmental and neuroprotective roles in metazoans. GDNF family ligands (GFLs) when bound to cognate GFRα co-receptors recognize and activate RET ...RET receptor tyrosine kinase plays vital developmental and neuroprotective roles in metazoans. GDNF family ligands (GFLs) when bound to cognate GFRα co-receptors recognize and activate RET stimulating its cytoplasmic kinase function. The principles for RET ligand-co-receptor recognition are incompletely understood. Here, we report a crystal structure of the cadherin-like module (CLD1-4) from zebrafish RET revealing interdomain flexibility between CLD2 and CLD3. Comparison with a cryo-electron microscopy structure of a ligand-engaged zebrafish RET-GDNF-GFRα1a complex indicates conformational changes within a clade-specific CLD3 loop adjacent to the co-receptor. Our observations indicate that RET is a molecular clamp with a flexible calcium-dependent arm that adapts to different GFRα co-receptors, while its rigid arm recognizes a GFL dimer to align both membrane-proximal cysteine-rich domains. We also visualize linear arrays of RET-GDNF-GFRα1a suggesting that a conserved contact stabilizes higher-order species. Our study reveals that ligand-co-receptor recognition by RET involves both receptor plasticity and strict spacing of receptor dimers by GFL ligands.
External linksStructure / PubMed:33484636 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.2 - 26.0 Å
Structure data

EMDB-11777:
RET/GDF15/GFRAL extracellular complex negative stain envelope
Method: EM (single particle) / Resolution: 26.0 Å

11822

7aml

EMDB-11822, PDB-7aml:
RET/GDNF/GFRa1 extracellular complex Cryo-EM structure
Method: EM (single particle) / Resolution: 3.5 Å

PDB-7ab8:
Crystal structure of a GDNF-GFRalpha1 complex
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7amk:
Zebrafish RET Cadherin Like Domains 1 to 4.
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER / Diethylene glycol

ChemComp-HOH:
WATER / Water

ChemComp-CA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-PGE:
TRIETHYLENE GLYCOL / Polyethylene glycol

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM / MES (buffer)

Source
  • Homo sapiens (human)
  • danio rerio (zebrafish)
KeywordsSIGNALING PROTEIN / VERTEBRATE DEVELOPMENT / PART OF THE RET-GFL-GFRA COMPLEX / NEUROTROPHIC FACTOR / Ligand recognition / receptor tyrosine kinase / glycosylation

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