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Peer-reviewedCC BY 4.0Biomolecules

Comparative Interactomics Identifies Conserved 14-3-3 Interactions and an Association of ANKRD55 with IFT-B in a Microglial Cell Model

3 more authors
10 affiliations
  1. 1Inflammation & Biomarkers Group, Biobizkaia Health Research Institute, 48903 Barakaldo, Spain
  2. 2Red de Enfermedades Inflamatorias (REI), Redes de Investigación Cooperativa Orientada a Resultados en Salud (RICORS), Carlos IIII Health Research Institute, 28029 Madrid, Spain
  3. 3Microscopy Facility, Biobizkaia Health Research Institute, 48903 Barakaldo, Spain
  4. 4Proteomics Platform, Center for Cooperative Research in Biosciences (CIC bioGUNE), Basque Research and Technology Alliance (BRTA), CIBERehd, Bizkaia Science and Technology Park, 48160 Derio, Spain
  5. 5Department of Immunology, Genetics and Pathology, Cancer Precision Medicine Research Unit, Rudbeck Laboratory, Uppsala University, 75185 Uppsala, Sweden
  6. 6Department of Neuroscience, Faculty of Medicine and Nursing, University of the Basque Country (EHU), 48940 Leioa, Spain
  7. 7Department of Physiology, Faculty of Medicine and Nursery, University of the Basque Country (EHU), 48940 Leioa, Spain
  8. 8Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan
  9. 9Biochemistry and Molecular Biology Department, Science and Technology School, University of the Basque Country (EHU), 48940 Leioa, Spain
  10. 10Ikerbasque, Basque Foundation for Science, 48009 Bilbao, Spain

Abstract

Ankyrin repeat domain-containing protein 55 (ANKRD55) is genetically associated with multiple sclerosis, but its cellular function remains incompletely defined. To investigate its potential role in neuroinflammatory pathways, we mapped ANKRD55-interacting proteins in neuroblastoma, astrocytic, microglial, and monocytic cell lines by affinity purification–mass spectrometry. Across all four cell lines, 14-3-3 isoforms were the most reproducible partners, whereas the IMhu-M microglial interactome uniquely contained eight intraflagellar transport complex B (IFT-B) components. In visible immunoprecipitation assays, IFT46–IFT56 was the smallest tested IFT-B subassembly sufficient to support detectable association with ANKRD55. Confocal microscopy localized endogenous ANKRD55 to pericentriolar material and basal bodies, but not to primary cilia, and identified partial association with P-body markers. These data distinguish a conserved 14-3-3 interaction core from cell-restricted centrosomal/IFT-B and RNP-associated ANKRD55 pools.

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BibTeX
@article{mena2026comparative,
  title = {{Comparative Interactomics Identifies Conserved 14-3-3 Interactions and an Association of ANKRD55 with IFT-B in a Microglial Cell Model}},
  author = {Jorge Mena and Raquel Tulloch-Navarro and Ainhoa Fiat-Arriola and Javier Díez-García and Mikel Azkargorta and Ane Aldekoa-Etxabe and Nerea Ugidos-Damboriena and Isabel Artiga-Folch and Cecilia Lindskog and Olatz Pampliega and Iraide Alloza-Moral and Yohei Katoh and Kazuhisha Nakayama and Felix Elortza and Koen Vandenbroeck van Caeckenbergh},
  journal = {Biomolecules},
  year = {2026},
  month = nov,
  doi = {10.3390/biom16111620},
  url = {https://www.mdpi.com/2218-273X/16/11/1620},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Comparative Interactomics Identifies Conserved 14-3-3 Interactions and an Association of ANKRD55 with IFT-B in a Microglial Cell Model
AU  - Jorge Mena
AU  - Raquel Tulloch-Navarro
AU  - Ainhoa Fiat-Arriola
AU  - Javier Díez-García
AU  - Mikel Azkargorta
AU  - Ane Aldekoa-Etxabe
AU  - Nerea Ugidos-Damboriena
AU  - Isabel Artiga-Folch
AU  - Cecilia Lindskog
AU  - Olatz Pampliega
AU  - Iraide Alloza-Moral
AU  - Yohei Katoh
AU  - Kazuhisha Nakayama
AU  - Felix Elortza
AU  - Koen Vandenbroeck van Caeckenbergh
PY  - 2026
DA  - 2026/11/06
JO  - Biomolecules
DO  - 10.3390/biom16111620
UR  - https://www.mdpi.com/2218-273X/16/11/1620
AB  - Ankyrin repeat domain-containing protein 55 (ANKRD55) is genetically associated with multiple sclerosis, but its cellular function remains incompletely defined. To investigate its potential role in neuroinflammatory pathways, we mapped ANKRD55-interacting proteins in neuroblastoma, astrocytic, microglial, and monocytic cell lines by affinity purification–mass spectrometry. Across all four cell lines, 14-3-3 isoforms were the most reproducible partners, whereas the IMhu-M microglial interactome uniquely contained eight intraflagellar transport complex B (IFT-B) components. In visible immunoprecipitation assays, IFT46–IFT56 was the smallest tested IFT-B subassembly sufficient to support detectable association with ANKRD55. Confocal microscopy localized endogenous ANKRD55 to pericentriolar material and basal bodies, but not to primary cilia, and identified partial association with P-body markers. These data distinguish a conserved 14-3-3 interaction core from cell-restricted centrosomal/IFT-B and RNP-associated ANKRD55 pools.
SN  - 2218-273X
ER  -