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ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome
Journal article   Peer reviewed

ISPD loss-of-function mutations disrupt dystroglycan O-mannosylation and cause Walker-Warburg syndrome

Tobias Willer, Hane Lee, Mark Lommel, Takako Yoshida-Moriguchi, Daniel Beltran Valero de Bernabe, David Venzke, Sebahattin Cirak, Harry Schachter, Jiri Vajsar, Thomas Voit, …
Nature genetics, Vol.44(5), pp.575-580
05/2012
DOI: 10.1038/ng.2252
PMCID: PMC3371168
PMID: 22522420
url
https://www.ncbi.nlm.nih.gov/pmc/articles/3371168View
Open Access

Abstract

Walker-Warburg syndrome (WWS) is clinically defined as congenital muscular dystrophy accompanied by a variety of brain and eye malformations. It represents the most severe clinical phenotype in a spectrum of alpha-dystroglycan posttranslational processing abnormalities, which share a defect in laminin binding glycan synthesis 1 . Although six WWS causing genes have been described, only half of all patients can currently be diagnosed genetically 2 . A cell fusion complementation assay using fibroblasts from undiagnosed WWS individuals identified five novel complementation groups. Further evaluation of one group by linkage analysis and targeted sequencing identified recessive mutations in the isoprenoid synthase domain containing ( ISPD ) gene. Confirmation of the pathogenicity of the identified ISPD mutations was demonstrated by complementation of fibroblasts with wild-type ISPD . Finally, we show that recessive mutations in ISPD abolish the initial step in laminin binding glycan synthesis by disrupting dystroglycan O -mannosylation. This establishes a novel mechanism for WWS pathophysiology.

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