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TitleStructural insights into the activation of the chicken ROS1 receptor by the NEL/NICOL ligand complex.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateFeb 24, 2026
AuthorsWeidong An / Xuewu Zhang / Xiao-Chen Bai /
PubMed AbstractThe receptor tyrosine kinase ROS1 plays essential roles in cell growth and sperm maturation, yet its activation mechanism has remained poorly understood. Here, we report high-resolution cryo-electron ...The receptor tyrosine kinase ROS1 plays essential roles in cell growth and sperm maturation, yet its activation mechanism has remained poorly understood. Here, we report high-resolution cryo-electron microscopy (cryo-EM) structures of chicken ROS1 in its ligand-free form, in complex with its ligand NEL, and with the ligand/co-ligand complex NEL/NICOL. Unliganded ROS1 adopts an arc-shaped conformation. The interaction between NEL and ROS1 is mediated by the VWC2 domain of NEL and the β1 domain of ROS1. Binding of NICOL to the coiled-coil domain of NEL stabilizes NEL into a batwing-shaped asymmetric dimer, which can recruit only one ROS1 molecule due to steric hindrance. Structural analyses and biochemical results suggest that the 2:1 NEL/NICOL complexes further oligomerize through LamG-VWC4 domain interactions, facilitating the clustering of multiple ROS1 for its activation. Functional assays confirm that both NICOL and the multimerization of NEL/NICOL complexes are required for robust ROS1 signaling. Our findings establish NICOL as a critical co-ligand for ROS1 and suggest a distinct ligand-driven oligomerization mechanism for ROS1 activation.
External linksNat Commun / PubMed:41735298 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 4.2 Å
Structure data

71042

9oyz

EMDB-71042, PDB-9oyz:
Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "head" region of chicken ROS1.
Method: EM (single particle) / Resolution: 2.9 Å

71047

9oz1

EMDB-71047, PDB-9oz1:
Cryo-EM structure of chicken ROS1 in apo-state. Cryo-EM refinement is focused on the "leg" region of chicken ROS1.
Method: EM (single particle) / Resolution: 3.6 Å

71049

9oz6

EMDB-71049, PDB-9oz6:
Cryo-EM structure of 1:1 chicken ROS1 and chicken NEL complex.
Method: EM (single particle) / Resolution: 2.7 Å

71051

9oz8

EMDB-71051, PDB-9oz8:
Cryo-EM structure of chicken NEL dimer bound with one human NICOL.
Method: EM (single particle) / Resolution: 4.1 Å

71057

9ozc

EMDB-71057, PDB-9ozc:
Cryo-EM structure of 1:2:1 ROS1/NEL/NICOL holo-complex, conformation 1.
Method: EM (single particle) / Resolution: 4.0 Å

71058

9ozh

EMDB-71058, PDB-9ozh:
Cryo-EM structure of 1:2:1 ROS1/NEL/NICOL holo-complex, conformation 2.
Method: EM (single particle) / Resolution: 4.2 Å

71059

9ozi

EMDB-71059, PDB-9ozi:
Cryo-EM structure of chicken ROS1 in apo-state. This is the complete map and model.
Method: EM (single particle) / Resolution: 3.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • gallus gallus (chicken)
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / ROS1 / SIGNALING PROTEIN / NEL

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