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 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
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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.
Bibliography:ObjectType-Article-1
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ISSN:1061-4036
1546-1718
DOI:10.1038/ng.2007.45