June 2015
Volume 56, Issue 7
Free
ARVO Annual Meeting Abstract  |   June 2015
Interactome analysis reveals that FAM161A is a component of the Golgi-centrosomal network
Author Affiliations & Notes
  • Pietro Farinelli
    Department of Medical Genetics, University of Lausanne, Lausanne, Switzerland
  • Silvio Alessandro Di Gioia
    Department of Medical Genetics, University of Lausanne, Lausanne, Switzerland
  • Stef Letteboer
    Department of Human Genetics and Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, Netherlands
  • Ronald Roepman
    Department of Human Genetics and Nijmegen Centre for Molecular Life Sciences, Radboud University Nijmegen Medical Centre, Nijmegen, Netherlands
  • Dror Sharon
    Department of Ophthalmology, Hadassah-Hebrew University Medical Center, Jerusalem, Israel
  • Yvan Arsenijevic
    Unit of Gene Therapy & Stem Cell Biology, Jules-Gonin Eye Hospital, University of Lausanne, Lausanne, Switzerland
  • Carlo Rivolta
    Department of Medical Genetics, University of Lausanne, Lausanne, Switzerland
  • Footnotes
    Commercial Relationships Pietro Farinelli, None; Silvio Alessandro Di Gioia, None; Stef Letteboer, None; Ronald Roepman, None; Dror Sharon, None; Yvan Arsenijevic, None; Carlo Rivolta, None
  • Footnotes
    Support None
Investigative Ophthalmology & Visual Science June 2015, Vol.56, 5505. doi:
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      Pietro Farinelli, Silvio Alessandro Di Gioia, Stef Letteboer, Ronald Roepman, Dror Sharon, Yvan Arsenijevic, Carlo Rivolta; Interactome analysis reveals that FAM161A is a component of the Golgi-centrosomal network. Invest. Ophthalmol. Vis. Sci. 2015;56(7 ):5505.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Purpose: Null mutations in FAM161A, which encodes a protein located in the photoreceptor connecting cilium/basal body, are the major cause of retinitis pigmentosa in the Israeli population. The function of FAM161A is unknown, but this protein has been shown to interact with a number of other proteins associated with inherited retinal dystrophies. In this study, we analyzed the binary interactome of FAM161A to elucidate its possible functions in retinal physiology and in retinitis pigmentosa.

Methods: We performed a saturated yeast-two-hybrid (Y2H) screen of human and bovine retinal cDNA libraries, using different fragments of FAM161A as baits. cDNA clones encoding putative interactors were evaluated by Sanger sequencing. Co-immunoprecipitation and proximity ligation assays (PLA) on cell lines were used to validate the newly-identified binary interactions.

Results: We identified as many as 53 partners of FAM161A, which revealed an interactome having a statistically significant bias towards proteins of the Golgi apparatus, the centrosome, and the microtubule network. The validation of FAM161A interactions with key partners by co-immunoprecipitation and PLAs strengthens our hypothesis that FAM161A is a member of the Golgi-centrosomal interactome, a network of proteins interconnecting Golgi maintenance, intracellular transport, and centrosome organization. Notable FAM161A interactors included AKAP9, FIP3, GOLGA3, KIFC3, KLC2, PDE4DIP, NIN, and TRIP11.

Conclusions: These findings suggest that FAM161A is at a center of a complex protein network and that its role is unlikely to be limited to ciliary tasks, but extend to more general cellular functions, highlighting possible novel mechanisms for the molecular pathology of retinal disease.

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