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

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...

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Published inNature 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
LanguageEnglish
Published United States Nature Publishing Group 01.01.2008
Subjects
Biochemistry
Cutis Laxa - genetics
Cutis Laxa - metabolism
Female
Genetics
Glycosylation
Golgi Apparatus
Humans
Infant
Male
Mutation
Proteins
Proton-Translocating ATPases - genetics
Skin diseases
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Summary: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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ISSN:1061-4036
1546-1718
DOI:10.1038/ng.2007.45