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The Ciliopathy Protein CC2D2A Associates with NINL and Functions in RAB8-MICAL3-Regulated Vesicle Trafficking.
Bachmann-Gagescu, Ruxandra; Dona, Margo; Hetterschijt, Lisette; Tonnaer, Edith; Peters, Theo; de Vrieze, Erik; Mans, Dorus A; van Beersum, Sylvia E C; Phelps, Ian G; Arts, Heleen H; Keunen, Jan E; Ueffing, Marius; Roepman, Ronald; Boldt, Karsten; Doherty, Dan; Moens, Cecilia B; Neuhauss, Stephan C F; Kremer, Hannie; van Wijk, Erwin.
Afiliación
  • Bachmann-Gagescu R; Institute for Molecular Life Sciences, University of Zurich, Zurich, Switzerland; Institute of Medical Genetics, University of Zurich, Zurich, Switzerland.
  • Dona M; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands.
  • Hetterschijt L; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands.
  • Tonnaer E; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • Peters T; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • de Vrieze E; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands.
  • Mans DA; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • van Beersum SE; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • Phelps IG; Department of Pediatrics, University of Washington, Seattle, Washington, United States of America.
  • Arts HH; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands; Department of Biochemistry, University of Western Ontario, London, Ontario, Canada.
  • Keunen JE; Department of Ophthalmology, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • Ueffing M; Division of Experimental Ophthalmology and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Germany.
  • Roepman R; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • Boldt K; Division of Experimental Ophthalmology and Medical Proteome Center, Centre for Ophthalmology, Eberhard Karls University Tuebingen, Germany.
  • Doherty D; Department of Pediatrics, University of Washington, Seattle, Washington, United States of America.
  • Moens CB; Fred Hutchinson Cancer Research Center, Seattle, Washington, United States of America.
  • Neuhauss SC; Institute for Molecular Life Sciences, University of Zurich, Zurich, Switzerland.
  • Kremer H; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands; Department of Human Genetics, Radboud University Medical Centre, Nijmegen, the Netherlands.
  • van Wijk E; Department of Otorhinolaryngology, Radboud University Medical Centre, Nijmegen, the Netherlands; Radboud Institute for Molecular Life Sciences, Radboud University Nijmegen, the Netherlands.
PLoS Genet ; 11(10): e1005575, 2015 Oct.
Article en En | MEDLINE | ID: mdl-26485645
Ciliopathies are a group of human disorders caused by dysfunction of primary cilia, ubiquitous microtubule-based organelles involved in transduction of extra-cellular signals to the cell. This function requires the concentration of receptors and channels in the ciliary membrane, which is achieved by complex trafficking mechanisms, in part controlled by the small GTPase RAB8, and by sorting at the transition zone located at the entrance of the ciliary compartment. Mutations in the transition zone gene CC2D2A cause the related Joubert and Meckel syndromes, two typical ciliopathies characterized by central nervous system malformations, and result in loss of ciliary localization of multiple proteins in various models. The precise mechanisms by which CC2D2A and other transition zone proteins control protein entrance into the cilium and how they are linked to vesicular trafficking of incoming cargo remain largely unknown. In this work, we identify the centrosomal protein NINL as a physical interaction partner of CC2D2A. NINL partially co-localizes with CC2D2A at the base of cilia and ninl knockdown in zebrafish leads to photoreceptor outer segment loss, mislocalization of opsins and vesicle accumulation, similar to cc2d2a-/- phenotypes. Moreover, partial ninl knockdown in cc2d2a-/- embryos enhances the retinal phenotype of the mutants, indicating a genetic interaction in vivo, for which an illustration is found in patients from a Joubert Syndrome cohort. Similar to zebrafish cc2d2a mutants, ninl morphants display altered Rab8a localization. Further exploration of the NINL-associated interactome identifies MICAL3, a protein known to interact with Rab8 and to play an important role in vesicle docking and fusion. Together, these data support a model where CC2D2A associates with NINL to provide a docking point for cilia-directed cargo vesicles, suggesting a mechanism by which transition zone proteins can control the protein content of the ciliary compartment.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 4_TD Problema de salud: 4_meningitis Asunto principal: Retina / Proteínas Nucleares / Proteínas / Cerebelo / Trastornos de la Motilidad Ciliar / Proteínas de Unión al GTP rab / Encefalocele / Oxigenasas de Función Mixta / Enfermedades Renales Poliquísticas / Proteínas Asociadas a Microtúbulos Tipo de estudio: Risk_factors_studies Idioma: En Revista: PLoS Genet Asunto de la revista: GENETICA Año: 2015 Tipo del documento: Article País de afiliación: Suiza

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Contexto en salud: 4_TD Problema de salud: 4_meningitis Asunto principal: Retina / Proteínas Nucleares / Proteínas / Cerebelo / Trastornos de la Motilidad Ciliar / Proteínas de Unión al GTP rab / Encefalocele / Oxigenasas de Función Mixta / Enfermedades Renales Poliquísticas / Proteínas Asociadas a Microtúbulos Tipo de estudio: Risk_factors_studies Idioma: En Revista: PLoS Genet Asunto de la revista: GENETICA Año: 2015 Tipo del documento: Article País de afiliación: Suiza
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