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. Epub 2007 Dec 23.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cutis Laxa / genetics*
  • Cutis Laxa / metabolism*
  • Female
  • Glycosylation
  • Golgi Apparatus
  • Humans
  • Infant
  • Male
  • Proton-Translocating ATPases / genetics*


  • ATP6V0A2 protein, human
  • Proton-Translocating ATPases