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

• Published in: Nature genetics Vol. 40; no. 1; pp. 32 - 34
• Main Authors: Rajab, Anna, van Bokhoven, Hans, Foulquier, Francois, Gruenewald, Stephanie, Lefeber, Dirk, Van Maldergem, Lionel, Morava, Eva, Reynders, Ellen, Urban, Zsolt, Wevers, Ron, Mundlos, Stefan, Annaert, Wim, Nürnberg, Peter, Kornak, Uwe, Dimopoulou, Aikaterini, van Reeuwijk, Jeroen, Fischer, Bjoern, Budde, Birgit, Brunner, Han G, Matthijs, Gert
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group US 01.01.2008; Nature Publishing Group
• Subjects: Agriculture; Animal Genetics and Genomics; Biochemistry; Biomedical and Life Sciences; Biomedicine; brief-communication; Cancer Research; Cutis Laxa - genetics; Cutis Laxa - metabolism; Female; Gene Function; Genetics; Glycosylation; Golgi Apparatus; Human Genetics; Humans; Infant; Male; Mutation; Proteins; Proton-Translocating ATPases - genetics; Skin diseases

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...