2. Academic Validation
  3. Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2

Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2

  • Nat Genet. 2008 Jan;40(1):32-4. doi: 10.1038/ng.2007.45.
Uwe Kornak 1,  Ellen Reynders,  Aikaterini Dimopoulou,  Jeroen van Reeuwijk,  Bjoern Fischer,  Anna Rajab,  Birgit Budde,  Peter Nürnberg,  Francois Foulquier,  ARCL Debré-type Study Group,  Dirk Lefeber,  Zsolt Urban,  Stephanie Gruenewald,  Wim Annaert,  Han G Brunner,  Hans van Bokhoven,  Ron Wevers,  Eva Morava,  Gert Matthijs,  Lionel Van Maldergem,  Stefan Mundlos
Affiliations

Affiliation

  • 1 Institute for Medical Genetics, Charité Universitaetsmedizin Berlin and Max Planck Institute for Molecular Genetics, Berlin, Germany. uwe.kornak@charite.de
PMID: 18157129 DOI: 10.1038/ng.2007.45
Abstract

We identified loss-of-function mutations in ATP6V0A2, encoding the a2 subunit of the V-type H+ ATPase, in several families with autosomal recessive cutis laxa type II or wrinkly skin syndrome. The mutations result in abnormal glycosylation of serum proteins (CDG-II) and cause an impairment of Golgi trafficking in fibroblasts from affected individuals. These results indicate that the a2 subunit of the Proton Pump has an important role in Golgi function.

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