| Literature DB >> 30057029 |
Anne Gregor1, Lynette G Sadleir2, Reza Asadollahi3, Silvia Azzarello-Burri3, Agatino Battaglia4, Lilian Bomme Ousager5, Paranchai Boonsawat3, Ange-Line Bruel6, Rebecca Buchert7, Eduardo Calpena8, Benjamin Cogné9, Bruno Dallapiccola10, Felix Distelmaier11, Frances Elmslie12, Laurence Faivre13, Tobias B Haack7, Victoria Harrison14, Alex Henderson15, David Hunt14, Bertrand Isidor16, Pascal Joset3, Satoko Kumada17, Augusta M A Lachmeijer18, Melissa Lees19, Sally Ann Lynch20, Francisco Martinez21, Naomichi Matsumoto22, Carey McDougall23, Heather C Mefford24, Noriko Miyake22, Candace T Myers24, Sébastien Moutton13, Addie Nesbitt25, Antonio Novelli10, Carmen Orellana21, Anita Rauch3, Monica Rosello21, Ken Saida22, Avni B Santani26, Ajoy Sarkar27, Ingrid E Scheffer28, Marwan Shinawi29, Katharina Steindl3, Joseph D Symonds30, Elaine H Zackai23, André Reis1, Heinrich Sticht31, Christiane Zweier32.
Abstract
Next-generation sequencing combined with international data sharing has enormously facilitated identification of new disease-associated genes and mutations. This is particularly true for genetically extremely heterogeneous entities such as neurodevelopmental disorders (NDDs). Through exome sequencing and world-wide collaborations, we identified and assembled 20 individuals with de novo variants in FBXO11. They present with mild to severe developmental delay associated with a range of features including short (4/20) or tall (2/20) stature, obesity (5/20), microcephaly (4/19) or macrocephaly (2/19), behavioral problems (17/20), seizures (5/20), cleft lip or palate or bifid uvula (3/20), and minor skeletal anomalies. FBXO11 encodes a member of the F-Box protein family, constituting a subunit of an E3-ubiquitin ligase complex. This complex is involved in ubiquitination and proteasomal degradation and thus in controlling critical biological processes by regulating protein turnover. The identified de novo aberrations comprise two large deletions, ten likely gene disrupting variants, and eight missense variants distributed throughout FBXO11. Structural modeling for missense variants located in the CASH or the Zinc-finger UBR domains suggests destabilization of the protein. This, in combination with the observed spectrum and localization of identified variants and the lack of apparent genotype-phenotype correlations, is compatible with loss of function or haploinsufficiency as an underlying mechanism. We implicate de novo missense and likely gene disrupting variants in FBXO11 in a neurodevelopmental disorder with variable intellectual disability and various other features.Entities:
Keywords: FBXO11; intellectual disability; neurodevelopmental disorder
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Year: 2018 PMID: 30057029 PMCID: PMC6080769 DOI: 10.1016/j.ajhg.2018.07.003
Source DB: PubMed Journal: Am J Hum Genet ISSN: 0002-9297 Impact factor: 11.025