| Literature DB >> 22366787 |
Jeroen K J Van Houdt1, Beata Anna Nowakowska, Sérgio B Sousa, Barbera D C van Schaik, Eve Seuntjens, Nelson Avonce, Alejandro Sifrim, Omar A Abdul-Rahman, Marie-José H van den Boogaard, Armand Bottani, Marco Castori, Valérie Cormier-Daire, Matthew A Deardorff, Isabel Filges, Alan Fryer, Jean-Pierre Fryns, Simone Gana, Livia Garavelli, Gabriele Gillessen-Kaesbach, Bryan D Hall, Denise Horn, Danny Huylebroeck, Jakub Klapecki, Malgorzata Krajewska-Walasek, Alma Kuechler, Matthew A Lines, Saskia Maas, Kay D Macdermot, Shane McKee, Alex Magee, Stella A de Man, Yves Moreau, Fanny Morice-Picard, Ewa Obersztyn, Jacek Pilch, Elizabeth Rosser, Nora Shannon, Irene Stolte-Dijkstra, Patrick Van Dijck, Catheline Vilain, Annick Vogels, Emma Wakeling, Dagmar Wieczorek, Louise Wilson, Orsetta Zuffardi, Antoine H C van Kampen, Koenraad Devriendt, Raoul Hennekam, Joris Robert Vermeesch.
Abstract
Nicolaides-Baraitser syndrome (NBS) is characterized by sparse hair, distinctive facial morphology, distal-limb anomalies and intellectual disability. We sequenced the exomes of ten individuals with NBS and identified heterozygous variants in SMARCA2 in eight of them. Extended molecular screening identified nonsynonymous SMARCA2 mutations in 36 of 44 individuals with NBS; these mutations were confirmed to be de novo when parental samples were available. SMARCA2 encodes the core catalytic unit of the SWI/SNF ATP-dependent chromatin remodeling complex that is involved in the regulation of gene transcription. The mutations cluster within sequences that encode ultra-conserved motifs in the catalytic ATPase region of the protein. These alterations likely do not impair SWI/SNF complex assembly but may be associated with disrupted ATPase activity. The identification of SMARCA2 mutations in humans provides insight into the function of the Snf2 helicase family.Entities:
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Year: 2012 PMID： 22366787 DOI： 10.1038/ng.1105
Source DB: PubMed Journal: Nat Genet ISSN： 1061-4036 Impact factor: 38.330