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@ARTICLE{Mariano:266342,
      author       = {Mariano, Vittoria and Kanellopoulos, Alexandros K. and
                      Ricci, Carlotta and Di Marino, Daniele and Borrie, Sarah C.
                      and Dupraz, Sebastian and Bradke, Frank and Achsel, Tilmann
                      and Legius, Eric and Odent, Sylvie and Billuart, Pierre and
                      Bienvenu, Thierry and Bagni, Claudia},
      title        = {{I}ntellectual {D}isability and {B}ehavioral {D}eficits
                      {L}inked to {CYFIP}1 {M}issense {V}ariants {D}isrupting
                      {A}ctin {P}olymerization},
      journal      = {Biological psychiatry},
      volume       = {95},
      number       = {2},
      issn         = {0006-3223},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {DZNE-2023-01127},
      pages        = {161 - 174},
      year         = {2024},
      abstract     = {15q11.2 deletions and duplications have been linked to
                      autism spectrum disorder, schizophrenia, and intellectual
                      disability. Recent evidence suggests that dysfunctional
                      CYFIP1 (cytoplasmic FMR1 interacting protein 1) contributes
                      to the clinical phenotypes observed in individuals with
                      15q11.2 deletion/duplication syndrome. CYFIP1 plays crucial
                      roles in neuronal development and brain connectivity,
                      promoting actin polymerization and regulating local protein
                      synthesis. However, information about the impact of single
                      nucleotide variants in CYFIP1 on neurodevelopmental
                      disorders is limited.Here, we report a family with 2
                      probands exhibiting intellectual disability, autism spectrum
                      disorder, spastic tetraparesis, and brain morphology defects
                      and who carry biallelic missense point mutations in the
                      CYFIP1 gene. We used skin fibroblasts from one of the
                      probands, the parents, and typically developing individuals
                      to investigate the effect of the variants on the
                      functionality of CYFIP1. In addition, we generated
                      Drosophila knockin mutants to address the effect of the
                      variants in vivo and gain insight into the molecular
                      mechanism that underlies the clinical phenotype.Our study
                      revealed that the 2 missense variants are in protein domains
                      responsible for maintaining the interaction within the wave
                      regulatory complex. Molecular and cellular analyses in skin
                      fibroblasts from one proband showed deficits in actin
                      polymerization. The fly model for these mutations exhibited
                      abnormal brain morphology and F-actin loss and recapitulated
                      the core behavioral symptoms, such as deficits in social
                      interaction and motor coordination.Our findings suggest that
                      the 2 CYFIP1 variants contribute to the clinical phenotype
                      in the probands that reflects deficits in actin-mediated
                      brain development processes.},
      keywords     = {Humans / Intellectual Disability: genetics / Actins:
                      genetics / Actins: metabolism / Autism Spectrum Disorder:
                      genetics / Autism Spectrum Disorder: metabolism /
                      Polymerization / Adaptor Proteins, Signal Transducing:
                      genetics / Fragile X Mental Retardation Protein: metabolism
                      / Actins (NLM Chemicals) / Actin remodeling (Other) / Autism
                      spectrum disorder (Other) / CYFIP1 (Other) / Drosophila
                      (Other) / Motor impairment (Other) / Social deficits (Other)
                      / Adaptor Proteins, Signal Transducing (NLM Chemicals) /
                      CYFIP1 protein, human (NLM Chemicals) / FMR1 protein, human
                      (NLM Chemicals) / Fragile X Mental Retardation Protein (NLM
                      Chemicals)},
      cin          = {AG Bradke},
      ddc          = {610},
      cid          = {I:(DE-2719)1013002},
      pnm          = {351 - Brain Function (POF4-351)},
      pid          = {G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37704042},
      doi          = {10.1016/j.biopsych.2023.08.027},
      url          = {https://pub.dzne.de/record/266342},
}