| Literature DB >> 7951315 |
T Glaser1, L Jepeal, J G Edwards, S R Young, J Favor, R L Maas.
Abstract
The human eye malformation aniridia results from haploinsufficiency of PAX6, a paired box DNA-binding protein. To study this dosage effect, we characterized two PAX6 mutations in a family segregating aniridia and a milder syndrome consisting of congenital cataracts and late onset corneal dystrophy. The nonsense mutations, at codons 103 and 353, truncate PAX6 within the N-terminal paired and C-terminal PST domains, respectively. The wild-type PST domain activates transcription autonomously and the mutant form has partial activity. A compound heterozygote had severe craniofacial and central nervous system defects and no eyes. The pattern of malformations is similar to that in homozygous Sey mice and suggests a critical role for PAX6 in controlling the migration and differentiation of specific neuronal progenitor cells in the brain.Entities:
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Year: 1994 PMID: 7951315 DOI: 10.1038/ng0894-463
Source DB: PubMed Journal: Nat Genet ISSN: 1061-4036 Impact factor: 38.330