De Novo Variants Disturbing the Transactivation Capacity of POU3F3 Cause a Characteristic Neurodevelopmental Disorder.

TitleDe Novo Variants Disturbing the Transactivation Capacity of POU3F3 Cause a Characteristic Neurodevelopmental Disorder.
Publication TypeJournal Article
Year of Publication2019
AuthorsBlok, LSnijders, Kleefstra, T, Venselaar, H, Maas, S, Kroes, HY, Lachmeijer, AMA, van Gassen, KLI, Firth, HV, Tomkins, S, Bodek, S, Õunap, K, Wojcik, MH, Cunniff, C, Bergstrom, K, Powis, Z, Tang, S, Shinde, DN, Au, C, Iglesias, AD, Izumi, K, Leonard, J, Tayoun, AAbou, Baker, SW, Tartaglia, M, Niceta, M, Dentici, MLisa, Okamoto, N, Miyake, N, Matsumoto, N, Vitobello, A, Faivre, L, Philippe, C, Gilissen, C, Wiel, L, Pfundt, R, Deriziotis, P, Brunner, HG, Fisher, SE
Corporate AuthorsDDD study
JournalAm J Hum Genet
Volume105
Issue2
Pagination403-412
Date Published2019 Aug 01
ISSN1537-6605
Abstract

POU3F3, also referred to as Brain-1, is a well-known transcription factor involved in the development of the central nervous system, but it has not previously been associated with a neurodevelopmental disorder. Here, we report the identification of 19 individuals with heterozygous POU3F3 disruptions, most of which are de novo variants. All individuals had developmental delays and/or intellectual disability and impairments in speech and language skills. Thirteen individuals had characteristic low-set, prominent, and/or cupped ears. Brain abnormalities were observed in seven of eleven MRI reports. POU3F3 is an intronless gene, insensitive to nonsense-mediated decay, and 13 individuals carried protein-truncating variants. All truncating variants that we tested in cellular models led to aberrant subcellular localization of the encoded protein. Luciferase assays demonstrated negative effects of these alleles on transcriptional activation of a reporter with a FOXP2-derived binding motif. In addition to the loss-of-function variants, five individuals had missense variants that clustered at specific positions within the functional domains, and one small in-frame deletion was identified. Two missense variants showed reduced transactivation capacity in our assays, whereas one variant displayed gain-of-function effects, suggesting a distinct pathophysiological mechanism. In bioluminescence resonance energy transfer (BRET) interaction assays, all the truncated POU3F3 versions that we tested had significantly impaired dimerization capacities, whereas all missense variants showed unaffected dimerization with wild-type POU3F3. Taken together, our identification and functional cell-based analyses of pathogenic variants in POU3F3, coupled with a clinical characterization, implicate disruptions of this gene in a characteristic neurodevelopmental disorder.

DOI10.1016/j.ajhg.2019.06.007
Alternate JournalAm. J. Hum. Genet.
PubMed ID31303265
PubMed Central IDPMC6698880
Grant ListT32 GM007748 / GM / NIGMS NIH HHS / United States
UM1 HG008900 / HG / NHGRI NIH HHS / United States