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TitleCryo-EM analyses reveal the common mechanism and diversification in the activation of RET by different ligands.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateSep 19, 2019
AuthorsJie Li / Guijun Shang / Yu-Ju Chen / Chad A Brautigam / Jen Liou / Xuewu Zhang / Xiao-Chen Bai /
PubMed AbstractRET is a receptor tyrosine kinase (RTK) that plays essential roles in development and has been implicated in several human diseases. Different from most of RTKs, RET requires not only its cognate ...RET is a receptor tyrosine kinase (RTK) that plays essential roles in development and has been implicated in several human diseases. Different from most of RTKs, RET requires not only its cognate ligands but also co-receptors for activation, the mechanisms of which remain unclear due to lack of high-resolution structures of the ligand/co-receptor/receptor complexes. Here, we report cryo-EM structures of the extracellular region ternary complexes of GDF15/GFRAL/RET, GDNF/GFRα1/RET, NRTN/GFRα2/RET and ARTN/GFRα3/RET. These structures reveal that all the four ligand/co-receptor pairs, while using different atomic interactions, induce a specific dimerization mode of RET that is poised to bring the two kinase domains into close proximity for cross-phosphorylation. The NRTN/GFRα2/RET dimeric complex further pack into a tetrameric assembly, which is shown by our cell-based assays to regulate the endocytosis of RET. Our analyses therefore reveal both the common mechanism and diversification in the activation of RET by different ligands.
External linksElife / PubMed:31535977 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 4.4 Å
Structure data

20572

6q2j

EMDB-20572, PDB-6q2j:
Cryo-EM structure of extracellular dimeric complex of RET/GFRAL/GDF15
Method: EM (single particle) / Resolution: 4.1 Å

EMDB-20573:
Cryo-EM structure of RET/GFRAL/GDF15 extracellular complex. The 3D refinement was focused on one of two halves with C1 symmetry applied.
Method: EM (single particle) / Resolution: 3.7 Å

20575

6q2n

EMDB-20575, PDB-6q2n:
Cryo-EM structure of RET/GFRa1/GDNF extracellular complex
Method: EM (single particle) / Resolution: 4.4 Å

20576

6q2o

EMDB-20576, PDB-6q2o:
Cryo-EM structure of RET/GFRa2/NRTN extracellular complex. The 3D refinement was applied with C2 symmetry.
Method: EM (single particle) / Resolution: 3.65 Å

EMDB-20577:
Cryo-EM structure of RET/GFRa2/NRTN extracellular complex. The 3D refinement was focused on one of two halves with C1 symmetry applied.
Method: EM (single particle) / Resolution: 3.4 Å

20578

6q2r

EMDB-20578, PDB-6q2r:
Cryo-EM structure of RET/GFRa2/NRTN extracellular complex in the tetrameric form
Method: EM (single particle) / Resolution: 4.3 Å

20579

6q2s

EMDB-20579, PDB-6q2s:
Cryo-EM structure of RET/GFRa3/ARTN extracellular complex. The 3D refinement was applied with C2 symmetry.
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-20580:
Cryo-EM structure of RET/GFRa3/ARTN extracellular complex. The 3D refinement was focused on one of two halves with C1 symmetry applied.
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

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

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsSIGNALING PROTEIN / RET / receptor tyrosine kinase / cryo-EM

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