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
  • 1. Institute for Medical Genetics, Charité Universitaetsmedizin Berlin and Max Planck Institute for Molecular Genetics, Berlin, Germany. [email protected]
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.