Predicted structure of the complete CPLANE complex reveals novel interactors and mechanisms of Jbts17 during ciliogenesis
- 1The University of Texas at Austin
Abstract
Cilia are highly conserved organelles that use hundreds of unique proteins to drive extracellular motility and serve as signaling hubs for eukaryotic cells. The Ciliogenesis and Planar Polarity Effector (CPLANE) protein complex controls basal body docking during early ciliogenesis and recruits the intraflagellar transport (IFT) proteins to the base of growing cilia. Leveraging recent advantages in deep learning neural networks and high-performance computing, we predict the structure of JBTS17, the largest CPLANE subunit, and the tertiary structure of the complete CPLANE complex, revealing direct contacts between JBTS17 and three other CPLANE members. We then used this model for an in silico protein-protein interaction screen that identified several novel JBTS17 interactors. Experiments in Xenopus confirmed a functional link in vivo between Jbts17 and the Spinocerebellar ataxia-associated protein TTBK2. The data provide new insights into mechanisms of CPLANE function during ciliogenesis and demonstrate the power of modeling protein complexes for the discovery of physical and functional protein interactions in cell homeostasis and disease.
Related
- Non-canonical alternate interactors of SARS CoV-2 Spike protein implicated in placental susceptibilty
- Predicted structure of the 89-kDa invasion-tip protein of Holospora obtusa, an endonuclear symbiont of Paramecium caudatum, suggests a pH-dependent conformational change
- Bacterial community structure and stable predicted functional profiles in the renal sac fluid of the cuttlefish Acanthosepion pharaonis
- Full-fat soybean origin and thermal processing affect protein secondary structure, in vitro digestion kinetics, and predicted standardized ileal amino acid digestibility in broiler chickens.
- Mutations That Matter: Domain-Specific Mutational Hotspots in BRCA1 and Its Key Interactors Differ Between TCGA and BCGA Breast Cancer Cohort-An In Silico Analysis.
BibTeX
@misc{gardner2026predicted,
title = {{Predicted structure of the complete CPLANE complex reveals novel interactors and mechanisms of Jbts17 during ciliogenesis}},
author = {T. P. Gardner and A. Prolomova and C. Lee and E. M. Marcotte and J. B. Wallingford},
howpublished = {bioRxiv},
year = {2026},
month = oct,
doi = {10.64898/2026.10.05.756796},
url = {https://www.biorxiv.org/content/10.64898/2026.10.05.756796v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Predicted structure of the complete CPLANE complex reveals novel interactors and mechanisms of Jbts17 during ciliogenesis
AU - T. P. Gardner
AU - A. Prolomova
AU - C. Lee
AU - E. M. Marcotte
AU - J. B. Wallingford
PY - 2026
DA - 2026/10/05
PB - bioRxiv
DO - 10.64898/2026.10.05.756796
UR - https://www.biorxiv.org/content/10.64898/2026.10.05.756796v1
AB - Cilia are highly conserved organelles that use hundreds of unique proteins to drive extracellular motility and serve as signaling hubs for eukaryotic cells. The Ciliogenesis and Planar Polarity Effector (CPLANE) protein complex controls basal body docking during early ciliogenesis and recruits the intraflagellar transport (IFT) proteins to the base of growing cilia. Leveraging recent advantages in deep learning neural networks and high-performance computing, we predict the structure of JBTS17, the largest CPLANE subunit, and the tertiary structure of the complete CPLANE complex, revealing direct contacts between JBTS17 and three other CPLANE members. We then used this model for an in silico protein-protein interaction screen that identified several novel JBTS17 interactors. Experiments in Xenopus confirmed a functional link in vivo between Jbts17 and the Spinocerebellar ataxia-associated protein TTBK2. The data provide new insights into mechanisms of CPLANE function during ciliogenesis and demonstrate the power of modeling protein complexes for the discovery of physical and functional protein interactions in cell homeostasis and disease.
ER -